Catalogue of lecture slides of Rodney Robert Porter

Bodleian Library, University of Oxford

C. Parker

2014

Department of Special Collections
Bodleian Library
Contact Information
Search Online Catalogues

Lecture slides of Rodney Robert Porter, c.1948-1960

Abstract:
110 glass slides of R.R. Porter (1917-1985), immunologist.

Shelfmarks: MS. Photogr. e. 66-70
Extent: 5 shelfmarks
Language of Material: English

Biographical History

Rodney Porter was born in Newton-le-Willows, Lancashire in 1917. He was educated at Ashton-in-Makerfield Grammar School (1928-1935) and Liverpool University (1935-1939), where he gained a first class degree in biochemistry. The second world war interrupted his post-graduate research at Liverpool and he saw active service in the Royal Artillery, Royal Engineers and the Royal Army Service Corps. On demobilization in 1946 he studied for his PhD under Fred Sanger in the department of biochemistry, at Cambridge, and it was here that he developed an interest in immunoglobulins. He married Julia Frances New, a research assistant in the physiology department at Cambridge, in 1948, and they had five children. After completing his PhD, he moved to the National Institute for Medical Research at Mill Hill, London in 1949. He was offered a position there by Thomas Work to pursue the interest of his own choice - the nature of antibody molecules. Although he made important advances during the period, notably the division of the molecule into three parts by papain digestion, in 1959 he still had little idea of the structure of the molecule (Bibliog. 15). In 1960 he was appointed to the first chair of immunology in Britain at the Wright-Fleming Institute at St Mary's Hospital Medical School in Paddington, London. His discovery of the 4-chain structure of antibody molecules in 1962 (Bibliog. 18-19) followed shortly after the demonstration by Geoffrey Edelman in the USA that antibodies were multichain proteins. He shared the Nobel Prize for Physiology or Medicine with Edelman in 1972 (Bibliog. 21). He was appointed the Whitley Professor of Biochemistry at Oxford in 1967 where his interests changed to the proteins of the complement system. He died tragically in a road accident in 1985, shortly before he was due to retire, at the age of 67.

Beside the Nobel Prize, Porter received many honours in his lifetime. He was elected a Fellow of the Royal Society in 1964, and received the Royal and Copley medals in 1973 and 1983 respectively. He was an honorary fellow of the Royal College of Physicians and of the Royal Society of Edinburgh, and shortly before his death he was made a Companion of Honour. He was elected to foreign membership of the National Academy of Sciences in 1972.

Further information can be found in the Dictionary of National Biography and Who Was Who.

Scope and Content

110 x 3.25 inch square double-glass slides which have the printing on the inner glass surface.


Note:

This catalogue was prepared using detailed notes provided by Dr Myer Salaman. He acknowledges the following, 'Some of the slides are difficult to interpret and I was greatly helped by Michael Crumpton, who worked in Porter's Department at St Mary's in the 1960s, and by Keith Gould and Alan Williamson. A few remain mysterious to us and maybe someone viewing the slides will be able to help.'

Arrangement

The arrangement is by Dr Salaman. Porter's numbering system has been retained: a running number followed by the year of production. Twelve slides have no year marked. Dr Salaman has divided the slides into two groups: group A directly concern antibodies or γ-globulin (the fraction of serum containing antibodies); group B relate to other proteins or techniques used in protein chemistry. Each group is arranged chronologically, with undated slides placed at the end of the appropriate group.

Bibliographical References

1) H. Svensson, 'Preparative electrophoresis and ionophoresis', Advances in Protein Chemistry, 4 (1948), 251-95

2) R.R. Porter, 'A chemical study of rabbit antiovalbumin', Biochemical Journal, 46.4 (Apr 1950), 473-8

3) R.R. Porter, 'The formation of a specific inhibitor by hydrolysis of rabbit antiovalbumin', Biochemical Journal, 46.4 (Apr 1950), 479-84

4) A.J. Martin and R.R. Porter, 'The chromatographic fractionation of ribonuclease', Biochemical Journal, 49.2 (Jul 1951), 215-8

5) H. Fraenkel-Conrat and R.R. Porter, 'The terminal amino groups of conalbumin, ovomucoid and avidin', Biochimica et Biophysica Acta, 9 (1952), 557-62

6) R.R. Porter, 'Partition chromatography of insulin and other proteins', Biochemical Journal, 53.2 (Jan 1953), 320-8

7) R.R. Porter, 'Chromatography of proteins', British Medical Bulletin, 10.3 (1954), 237-41

8) R.R. Porter, 'The fractionation of rabbit γ-globulin by partition chromatography', Biochemical Journal, 59.3 (Mar 1955), 405-10

9) O. Smithies, 'Zone electrophoresis in starch gels: group variations in the serum proteins of normal human adults', Biochemical Journal, 61.4 (Dec 1955), 629-41

10) R.R. Porter, 'The partition chromatography of enzymes', Methods in Enzymology, 1 (1955), 98-112

11) J.H. Humphrey and R.R. Porter, 'An investigation on rabbit antibodies by the use of partition chromatography', Biochemical Journal, 62.1 (Jan 1956), 93-9

12) R.R. Porter and E.M. Press, 'The fractionation of bovine γ-globulin by partition chromatography', Biochemical Journal, 66.4 (Aug 1957), 600-3

13) R.R. Porter, 'The isolation and properties of a fragment of bovine-serum albumin which retains the ability to combine with rabbit antiserum', Biochemical Journal, 66.4 (Aug 1957), 677-86

14) R.R. Porter, 'Separation and isolation of fractions of rabbit γ-globulin containing the antibody and antigenic combining sites', Nature, 182 (6 Sep 1958), 670-1

15) R.R. Porter, 'The hydrolysis of rabbit γ-globulin and antibodies with crystalline papain', Biochemical Journal, 73.1 (Sep 1959), 119-26

16) E.M. Press, R.R. Porter and J. Cebra, 'The isolation and properties of a proteolytic enzyme, cathepsin D, from bovine spleen', Biochemical Journal, 74.3 (Mar 1960), 501-14

17) F.W. Brambell, W.A. Hemmings, C.L. Oakley and R.R. Porter, 'The relative transmission of the fractions of papain hydrolyzed homologous γ-globulin from the uterine cavity to the foetal circulation in the rabbit', Proceedings of the Royal Society, B, 151 (1960), 478-82

18) 'The structure of gammaglobulins and antibodies' in Symposium on basic problems in neoplastic disease, ed. by A. Gellhorn and E. Hirschberg (Columbia University Press, 1962), 177-94

19) J.B. Fleischman, R.R. Porter and E.M. Press, 'The arrangement of the peptide chains in γ-globulin', Biochemical Journal, 88.2 (Aug 1963), 220-8

20) R.R. Porter, 'The structure of the heavy chain of immunoglobulin and its relevance to the nature of the antibody-combing site', Biochemical Journal, 105.2 (Nov 1967), 417-26

21) R.R. Porter, 'Structural studies of immunoglobulins', Nobel Lecture, 12 Dec 1972

Custodial History

The slides date from Porter's time at Mill Hill and the majority of them are labelled, 'Medical Research Council. National Institute for Medical Research, Mill Hill, London, N.W.7'. When Porter left St Mary's for Oxford, he left the slides behind, and they were later taken into the custody of Dr Salaman.

Acquisition

Donated by Dr Myer Salaman, Department of Immunology, St Mary's Campus of Imperial College School of Medicine, Norfolk Place, London, W2 1PG, June 2013, with the approval of Mrs Julia Porter, the widow of R.R. Porter.

Related Material

The Bodleian Library also holds the papers and correspondence of R.R. Porter, 1933-1986, which were catalogued by the Contemporary Scientific Archives Centre in 1987 (CSAC 119.1.87): MSS. Eng. misc. c. 995-1011, d. 1398-1434, e. 1534-6.

Preferred Form of Citation

Oxford, Bodleian Library, MS. Photogr. e. 66

Personal names (NCA Rules)

Porter | Rodney Robert | 1917-1985 | biochemist

Subjects (LCSH)

Molecular immunology

Descriptive List



Group A - slides involving antibodies or γ-globulins
Date: 1954-1956
Shelfmark: MS. Photogr. e. 66
Extent: 27 slides

Scope and Content:

Porter's numbering system has been retained: the first figure is a running number and the second figure represents the year.

  • (437/54) 'Repeat run of fractions', fig. 3 in R.R. Porter, 'The fractionation of rabbit γ-globulin by partition chromatography' (Bibliog. 8). Re-run fractions run true. The γ-globulin had been prepared from rabbit serum by sodium sulphate precipitation. [partial crack, upper left]
  • (439/54) 'Normal and immune ɤ globulins', fig. 4 in R.R. Porter, 'The fractionation of rabbit γ-globulin by partition chromatography' (Bibliog. 8). Partition chromatography of normal and immune rabbit γ-globulin. Starting at the top, the data can be read as follows: panel a, before immunization; panel b, early in immunization; panels c and d, later in immunization. Antibody produced early on (presumably IgM) fractionates differently from that produced later.
  • (440/54) Adsorption of antigen by immune globulin (process unknown) compared with that by other proteins. Specific adsorption best seen at low ionic strength.
  • (442/54) Adsorption of antigen by immune globulin (process unknown) compared with that by other proteins. Specific binding best observed around pH 7.
  • (324-333/55) J.H. Humphrey and R.R. Porter, 'An investigation on rabbit antibodies by the use of partition chromatography', (Bibliog. 11). Following partition chromatography of rabbit γ-globulin the distribution of protein in the peak is different from that of specific antibody activity. The position of the antibody is dependent on the antigen used, time after immunization and route of administration. The columns show antibody activity. In general early antibody (IgM) runs slower than later antibody (IgG). Ten slides, illustrating figures 1-10 in the above article:
    • (324/55) 'Fractionation of about 50 mg γ-globulin from rabbits after first course of intravenous injections with influenza virus type A', fig. 5
    • (325/55) 'Fractionation of about 50 mg γ-globulin from a rabbit three months after intramuscular injection of ovalbumin and adjuvant', fig. 10
    • (326/55) 'Fractionation of about 50 mg γ-globulin from rabbit no. 50 after third course of intravenous injection with killed pneumococcus', fig. 3
    • (327/55) 'Fractionation of about 50 mg γ-globulin from rabbit no. 50 after second course of intravenous injection with killed pneumococcus', fig. 2
    • (328/55) 'Fractionation of about 50 mg γ-globulin from rabbit no. 50 after first course of intravenous injections with killed pneumococcus', fig. 1
    • (329/55) 'Fractionation of about 50 mg γ-globulin from rabbit no. 50 after fifth course of intravenous injection with killed pneumococcus', fig. 4
    • (330/55) 'Fractionation of about 50 mg γ-globulin from rabbits after second course of intravenous injections with influenza virus type A', fig. 6
    • (331/55) 'Fractionation of about 50 mg γ-globulin from a rabbit which had a prolonged series of intravenous injections of alum-precipitated ovalbumin and six injections of killed pneumococci in the previous two weeks', fig. 7
    • (332/55) 'Fractionation of about 50 mg γ-globulin from rabbit one month after intramuscular injection of ovalbumin and adjuvant', fig. 8
    • (333/55) 'Fractionation of about 50 mg γ-globulin five months after intramuscular injection of ovalbumin and adjuvant', fig. 9
  • (437/55) 'Repeat run of fractions', fig. 3 in R.R. Porter, 'The fractionation of rabbit γ-globulin by partition chromatography' (Bibliog. 8). Re-run fractions run true. The γ-globulin had been prepared from rabbit serum by sodium sulphate precipitation. [copy of 437/54]
  • (667/55) 'Average amino acid composition of rabbit antibodies'
  • (669/55) Electrophoretic separation of rabbit serum into albumin and α, β and γ-globulins. Following immunisation there is a dramatic increase in the γ-globulin fraction showing that antibodies are γ-globulins.
  • (68/56) 'Zone electrophoresis' of serum globulin following biosynthetic radioactive labelling of proteins; see following slide 69/56. The continuous line shows absorption and the columns show radioactivity.
  • (69/56) 'Spleen from immune rabbit', with and without antibody. It seems that pieces of spleen from an immunised rabbit have been cultured in the presence of a radioactive amino acid such as 35S-methionine. The γ-globulin in the supernatant was isolated and further fractionated. The upper graph shows the radioactive labelling (broken line). The lower graph shows a fall in radioactivity on removal of antibody by combination with antigen, thereby confirming that the antibody had been labelled.
  • (379-387/56) R.R. Porter and E.M. Press, 'The fractionation of bovine γ-globulin by partition chromatography' (Bibliog. 12). Four slides illustrating figures 1-2 and tables 1-2:
    • (379/56) 'Table 2. N-terminal amino acids of Bovine γ-Globulin in Fractions'; it is now known that four moles of amino acids should have been expected per mole of protein, not less than one; see slide NY-1 below.
    • (381/56) 'Table 1. N-terminal amino acids of Bovine γ-Globulin'; see slide NY-1 below.
    • (386/56) Partition 'Chromatography of bovine γ-globulin', fig. 1, re-run fractions run true; see slides 439/54 and 714/58.
    • (387/56) Partition 'Chromatography of bovine γ-globulin', fig. 2; letters correspond to fractions used in table 2.
  • (478-481/56) R.R. Porter, 'The isolation and properties of a fragment of bovine-serum albumin which retains the ability to combine with rabbit antiserum' (Bibliog. 13). Four of six slides illustrating experiments in this article [a further two slides can be found in the next box, MS. Photogr. e. 67]:
    • (478/56) 'Comparison of behaviour of bovine-serum albumin (BSA) and inhibitor (I) on diffusion into antiserum in agar gel by the method of Ouchterlony (1953)', plate 1. The fragment (inhibitor) was about one fifth the size of the intact molecule and had the capacity to inhibit the precipitation of the intact antigen by antibody. Despite this ability to inhibit, some precipitation of the fragment itself was seen. Antibody not combing with the fragment formed a spur with the intact antigen.
    • (479/56) 'Reaction of inhibitor with serum 1b', fig. 4, shows inhibition of reaction between rabbit anti-BSA and BSA (top line) and goat serum albumin (bottom line)
    • (480/56) 'Purification of inhibitor', shortened version of scheme 1, purification of fragment
    • (481/56) 'Amino acid analysis', table 1, amino acid analysis of fragment and bovine serum albumin

Group A - slides involving antibodies or γ-globulins
Date: 1956-1959
Shelfmark: MS. Photogr. e. 67
Extent: 28 slides

Scope and Content:

Porter's numbering system has been retained: the first figure is a running number and the second figure represents the year.

  • (485-486/56) R.R. Porter, 'The isolation and properties of a fragment of bovine-serum albumin which retains the ability to combine with rabbit antiserum' (Bibliog. 13). Two of six slides illustrating experiments in this article:
    • (485/56) Elution diagram of 'Zone electrophoresis', fig. 1, column zone electrophoresis of fragment showing inhibitory activity in slowest fraction; delay in flocculation (closed circles) measured by eye or by optical density
    • (486/56) 'Reaction of inhibitor with serum 1a', fig. 3, fragment showed some precipitation (filled circles) and material not precipitated retained some inhibitory action (open squares)
  • (484/56) 'Fractionation of human γ-globulin', probably by column zone electrophoresis; fraction 1 is presumably the purified γ-globulin; Porter did not publish on human antibodies in this period.
  • (448/57) 'Fig. 1. Two-dimensional electrophoresis of normal human serum of group IIB', showing good separation of γ-globulin. For human serum groups see O. Smithies, 'Zone electrophoresis in starch gels: group variations in the serum proteins of normal human adults' (Bibliog. 9)
  • (286/58) 'Molecular weights of antibodies', sedimentation coefficients and molecular weights of antibodies; indicates existence of two kinds of antibody (IgM and IgG).
  • (289/58) 'Chromatography of papain digested γ-globulin on CM [carboxymethyl] cellulose', an earlier version of the key finding shown in slide 24/59 below.
  • (714/58) Fractions from partition chromatography run true; possibly bovine γ-globulin (see slide 386/56 above)
  • (21-25/59, 72-73/59, 75/59) R.R. Porter, 'The hydrolysis of rabbit γ-globulin and antibodies with crystalline papain' (Bibliog. 15); eight slides to illustrate this article:
    • (24/59) 'Chromatography of Digest on CM Cellulose', fig. 1; fractionation of papain-digested rabbit γ-globulin on carboxymethylcellulose, a key step in determining the 4-chain structure of antibodies. Three fractions (I, II and III) were revealed. Fractions I and II could bind to antigen as evidenced by their inhibition of binding by the intact molecule. They were later shown to be near identical in structure with only minor charge differences, and it is remarkable that this charge heterogeneity among different antibody molecules sorts itself into two separate peaks rather than one broad peak. They represent what is now known as the antibody Fab fragments of which there are two per mole of antibody. Fraction III is known as the Fc fragment, and possesses other antibody properties (see slide 330/60 below). Unlike Fab its structure does not very according to antibody specificity, and was found to form crystals (see slide NY-12 below).
    • (23/59) 'Inhibition of Precipitation by I and II (Anti HSA [Human Serum Albumin])', fig. 3; Fractions I and II interfere with binding of antigen by undigested antibody
    • (22/59) 'Inhibitory Power of II from Anti SSS III and Anti HSA [Human Serum Albumin]', fig. 4; Fraction II interferes with binding of antigen by undigested antibody [slide cracked across middle and held with sellotape]
    • (21/59) 'Precipitin Curve of I, II and III with Rat Anti II Serum', fig. 5; precipitation of fractions by antibody to Fraction II. The antibody precipitated Fractions I and II but not Fraction III. The antigenic properties of these fractions proved of great help in establishing the 4-chain structure.
    • (25/59) 'Different ways of splitting rabbit γ-globulin to give three fractions of approximately equal size', fig. 6; speculative structure of a single chain antibody molecule [slide cracked lower left]
    • (75/59) 'Amino acid analysis of fragments from non-immune serum', table 2; amino acid analysis of fractions
    • (73/59) 'Recovery of amino acid residues', table 3; amino acid analysis of γ-globulin and fractions
    • (72/59) 'Carbohydrate content of γ-globulin and fractions', table 4
  • (518-529/59) E.M. Press, R.R. Porter and J. Cebra, 'The isolation and properties of a proteolytic enzyme, cathepsin D, from bovine spleen' (Bibliog. 16); research on proteolytic activity in bovine spleen to determine the fate of antibodies in an antibody-forming organ, which led to the discovery of the enzyme cathepsin D; thirteen of fifteen slides [remaining 2 slides are in MS. Photogr. e. 68], comprising:
    • (518/59) 'Preparation of cathepsin D from 1 kg minced spleen'
    • (519/59) 'Rechromatography on DEAE borate / phosphate buffer 0.00875M pH 8.4'
    • (520/59) 'Hydrolysis of carbobenzoxy-glutamyl-tyrosine at 37°C'
    • (521/59) 'Chromatgography of the α form of Cathepsin D on CM at pH 5.5'
    • (522/59) 'Chromatography on CM at pH 5.5'
    • (523/59) 'pH stability of cathepsin D at 37°C'
    • (524/59) 'Chromatography of the β form of cathepsin D on CM at pH 5.5'
    • (525/59) 'Hydrolysis of the B chain of insulin'
    • (526/59) 'Rechromatography on DEAE borate-phosphate buffer 0.00875M pH 8.4'
    • (527/59) 'pH optimum of cathepsin D'
    • (528/59) 'Starch gel electrophoresis'
    • (528/59) 'Starch gel electrophoresis', showing only pH 8.0
    • (529/59) 'Comparison of different spleens'

Group A - slides involving antibodies or γ-globulins
Date: c.1948-1960
Shelfmark: MS. Photogr. e. 68 [part of]
Extent: 18 slides

Scope and Content:

Porter's numbering system has been retained: the first figure is a running number and the second figure represents the year.

  • (530-531/59) E.M. Press, R.R. Porter and J. Cebra, 'The isolation and properties of a proteolytic enzyme, cathepsin D, from bovine spleen' (Bibliog. 16); research on proteolytic activity in bovine spleen to determine the fate of antibodies in an antibody-forming organ, which led to the discovery of the enzyme cathepsin D; two of fifteen slides [previous 13 slides are in MS. Photogr. e. 67], comprising:
    • (530/59) 'Chromatography of cathepsin D on DEAE borate phosphate buffer pH 8.4'
    • (531/59) 'Chromatography of cathepsin D on DEAE borate phosphate buffer pH 8.4' [graph enlarged]
  • (287/60) 'Inhibition of precipitation with anti-HSA digest', fig. 2 in R.R. Porter, 'Separation and isolation of fractions of rabbit γ-globulin containing the antibody and antigenic combining sites' (Bibliog. 14). Precipitation of human serum albumin (HSA) by rabbit antibody to HSA is inhibited by a papain digest of the antibody. The digest has no effect on the equivalent bovine albumin system.
  • (328/60) 'Transmission of γ-globulin and antitoxin across the 24 day foetal yolk-sac membrane', simplified version of table 2 in F.W. Brambell, W.A. Hemmings, C.L. Oakley and R.R. Porter, 'The relative transmission of the fractions of papain hydrolyzed homologous γ-globulin from the uterine cavity to the foetal circulation in the rabbit' (Bibliog 17). Slide shows extent of the transmission of γ-globulin and fractions across the rabbit foetal yolk-sac membrane. This is the original evidence that placental transfer of antibody molecules is dictated by the Fc component. Fab fragments are not transferred. Pepsin digestion removes Fc leaving a double Fab fragment.
  • (329/60) 'Sedimentation coefficient after peptic digestion', in the presence of cysteine there is further breakdown of the double Fab to single Fab fragments.
  • (330/60) 'Distribution of properties of antibody fractions', the different properties of Fab and Fc fragments of γ-globulin
  • (NY-1-2) R.R. Porter, 'A chemical study of rabbit antiovalbumin' (Bibliog. 2); two slides, [c.1950], comprising:
    • (NY-1) 'Endgroup assay of rabbit γ-globulin', table 1. One molecule of N-terminal amino acid (alanine) was found per molecule of antibody / γ-globulin. This misled Porter into thinking he was dealing with a single chain protein. We now know that the N-terminal of the heavy chains is glutamic acid which hides its amino group as pyrrolidonecarboxylic acid. Kappa light chains have alanine as N-terminal but it is not clear why two molecules were not found. Lamda light chains are a minor component in the rabbit.
    • (NY-2) 'Terminal peptides of γ-globulin', table 3; terminal alanine peptides of rabbit antibody / γ-globulin. In total one alanine N-terminal per molecule (molecular weight should read 160,000).
  • (NY-3-5) R.R. Porter, 'The formation of a specific inhibitor by hydrolysis of rabbit antiovalbumin' (Bibliog. 3); three slides, [c.1950], representing early evidence that one can separate the binding site from other parts of the antibody molecule [see slide 24/59 above], comprising:
    • (NY-3) 'Flocculation rate in presence of inhibitor', fig. 1; papain-treated rabbit antiovalbumin inhibits interaction of intact antibody and antigen
    • (NY-4) 'Flocculation rates with varying antibody and inhibitor concentration', fig. 2; increasing inhibitor concentration results in greater inhibition of flocculation
    • (NY-5) 'Reversal of flocculation', table 2; inhibitor can cause dissociation of antigen / antibody complex
  • (NY-6-10) early experiments investigating the reactivity of lysine ε-NH2 groups in various proteins with fluorodinitrobenzene. Probably from Porter's PhD thesis, 'The free amino groups of proteins' (Cambridge University, 1948). Horse pseudoglobulin presumably refers to that fraction of horse serum prepared as for bovine globulin. Five slides, comprising:
    • (NY-6) 'Lysine ε-NH2 Groups reacting with DNFB / Native Proteins'
    • (NY-7) 'Lysine ε-NH2 Groups Reacting with DNFB / Denatured Proteins'
    • (NY-8) 'Table I. Details of the protein preparations'
    • (NY-9) 'Table III. The number of ε-NH2 groups acetylated by ketene or acetic anhydride'
    • (NY-10) 'Table V. The denaturation of β lactoglobulin by ethanol'
  • (NY-11) 'Table 9. The specific action of antihaemoglobin serums', species specificity of antibodies to haemoglobin, probably made in rabbits. Results taken from L. Hetkoen and A.K. Boor who were publishing in the 1930s.
  • (NY-12) 'Crystalline fraction III x 1150', crystals of Fc [see slide 24/59 above]

Group B - slides relating to other proteins or techniques used in protein chemistry
Date: 1950-1952
Shelfmark: MS. Photogr. e. 68 [part of]
Extent: 9 slides

Scope and Content:

As above, Porter's numbering has been retained: the first figure is a running number and the second figure represents the year.

  • (112/50) N-terminal amino acids and reactive lysine determination using fluorodinitrobenzene
  • (113/50) 'The numbers of free amino groups of haemoglobins', N-terminal amino acids and numbers of lysines in haemoglobins of different species
  • (259-262/51) H. Fraenkel-Conrat and R.R. Porter, 'The terminal amino groups of conalbumin, ovomucoid and avidin' (Bibliog. 5), a study of N-terminal amino acids and lysine numbers in conalbumin, ovomucoid and avidin; four slides, comprising:
    • (259/51) 'Free amino groups of avidin', relates to data in table 4
    • (260/51) 'Loss on hydrolysis (% recovery)', relates to data in table 1
    • (261/51) 'Free amino groups of ovomucoid', relates to data in table 3
    • (262/51) 'Free amino groups of conalbumin', relates to data in table 2
  • (210/52 and 212/52) R.R. Porter, 'Partition chromatography of insulin and other proteins' (Bibliog. 6); partition chromatography of different preparations of crude insulin; two slides, comprising:
    • (210/52) 'Chromatography of crude insulin C', fig. 5
    • (212/52) 'Chromatography of crude insulin A', fig. 3
  • (433/52) 'Chymotrypsin activated by trypsin', separation of chymotrypsin from chymotrypsinogen; method not identified but apparently not partition chromatography [compare Bibliog. 10, fig. 9]

Group B - slides relating to other proteins or techniques used in protein chemistry
Date: 1952-1959
Shelfmark: MS. Photogr. e. 69
Extent: 28 slides

Scope and Content:

As above, Porter's numbering has been retained: the first figure is a running number and the second figure represents the year.

  • (434/52, 436-7/52) Three slides of phase diagrams similar to those illustrated by R.R. Porter, 'The partition chromatography of enzymes' (Bibliog. 10). Such phase diagrams are obtained by mixing water, salt and organic solvent in different proportions and looking for the appearance of opalescence. The aim is to find optimal conditions for partition chromatography.
  • (287/53) Partition 'Chromatogram of ribonuclease', fig. 2 in A.J. Martin and R.R. Porter, 'The chromatographic fractionation of ribonuclease' (Bibliog. 4)
  • (288/53) 'Crude penicillinase', partition chromatography of the enzyme, penicillinase; fig. 11 in R.R. Porter, 'The partition chromatography of enzymes' (Bibliog. 10)
  • (289/53) 'Phase diagram of the system ammonium sulphate-water-ethylene glycol monoethyl ether at 20°', fig. 1 in A.J. Martin and R.R. Porter, 'The chromatographic fractionation of ribonuclease' (Bibliog. 4)
  • (290/53) 'Crystalline trypsin', partition chromatography of the enzyme, trypsin; fig. 10 in R.R. Porter, 'The partition chromatography of enzymes' (Bibliog. 10)
  • (291/53) Partition 'Chromatograms of ribonuclease', fig. 3 in A.J. Martin and R.R. Porter, 'The chromatographic fractionation of ribonuclease' (Bibliog. 4)
  • (292/53) 'Activated chymotrypsinogen', partition chromatography of the activated enzyme, fig. 9 in R.R. Porter, 'The partition chromatography of enzymes' (Bibliog. 10)
  • (411/54) 'Separation of ribonuclease from crude extract of beef pancreas', ion exchange chromatography of the enzyme, ribonuclease; fig. 2 in R.R. Porter, 'Chromatography of proteins' (Bibliog. 7)
  • (413/54) ion exchange chromatography of the enzyme, chymotrypsinogen
  • (415/54) 'Fractionation of lysozyme carbonate on amberlite IRC-50', ion exchange chromatography of the enzyme, lysozyme; fig. 3 in R.R. Porter, 'Chromatography of proteins' (Bibliog. 7)
  • (417/54) elution of unidentified proteins at increasing sodium chloride molarity; probably adsorption chromatography - see Bibliog. 7
  • (441/54) system for partition chromatography at sub-zero temperatures
  • (443/54) identical to slide 417/54 above
  • (70/57) demonstration of column chromatography; hand-coloured photograph of equipment
  • (71/57) 'Electropherogram of a mixture of various "neutral" amino acids obtained by electrophoresis...', electrophoretic separation of 'neutral' amino acids
  • (72/57) purified protein, not identified
  • (73/57) diagram of apparatus, unidentified
  • (74/57) 'Stratification phenomenon (Blank and Valkó, 1928)', stratification in electrophoresis [see Bibliog. 1]
  • (76/57) 'Diagram illustrating principle of the method' for continuous electrophoresis
  • (77/57) photograph of system for electrophoresis
  • (88/57) possibly continuous electrophoresis with added concentration gradient
  • (334/57) 'Table 3. N-terminal amino acids of bovine β-globulin', R.R. Porter and E.M. Press, 'The fractionation of bovine γ-globulin by partition chromatography' (Bibliog. 12)
  • (349/57) fractionation of radioactive, unidentified protein
  • (288/58) 'N-terminal sequence of rabbit α globulin'
  • (5/59) 'Arrangement for continuous removal of zones during electrophoresis', diagram of column zone electrophoresis
  • (6/59) 'Electropherogram of a mixture of basic peptides of the posterior lobe of pig pituitary'

Three original slide boxes, labelled by Porter
Date: n.d.
Shelfmark: MS. Photogr. e. 70

Transformation from XML to HTML by Lawrence Mielniczuk
11 August 2014