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Group A - slides involving antibodies or γ-globulins, 1956-1959

MS. Photogr. e. 67

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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:
  1. (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
  2. (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:
  1. (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).
  2. (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
  3. (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]
  4. (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.
  5. (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]
  6. (75/59) 'Amino acid analysis of fragments from non-immune serum', table 2; amino acid analysis of fractions
  7. (73/59) 'Recovery of amino acid residues', table 3; amino acid analysis of γ-globulin and fractions
  8. (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:
  1. (518/59) 'Preparation of cathepsin D from 1 kg minced spleen'
  2. (519/59) 'Rechromatography on DEAE borate / phosphate buffer 0.00875M pH 8.4'
  3. (520/59) 'Hydrolysis of carbobenzoxy-glutamyl-tyrosine at 37°C'
  4. (521/59) 'Chromatgography of the α form of Cathepsin D on CM at pH 5.5'
  5. (522/59) 'Chromatography on CM at pH 5.5'
  6. (523/59) 'pH stability of cathepsin D at 37°C'
  7. (524/59) 'Chromatography of the β form of cathepsin D on CM at pH 5.5'
  8. (525/59) 'Hydrolysis of the B chain of insulin'
  9. (526/59) 'Rechromatography on DEAE borate-phosphate buffer 0.00875M pH 8.4'
  10. (527/59) 'pH optimum of cathepsin D'
  11. (528/59) 'Starch gel electrophoresis'
  12. (528/59) 'Starch gel electrophoresis', showing only pH 8.0
  13. (529/59) 'Comparison of different spleens'


  • 1956-1959


28 items


MS. Photogr. e. 67

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