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Group A - slides involving antibodies or γ-globulins, 1954-1956

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MS. Photogr. e. 66

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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.

Includes:

(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:
  1. (324/55) 'Fractionation of about 50 mg γ-globulin from rabbits after first course of intravenous injections with influenza virus type A', fig. 5
  2. (325/55) 'Fractionation of about 50 mg γ-globulin from a rabbit three months after intramuscular injection of ovalbumin and adjuvant', fig. 10
  3. (326/55) 'Fractionation of about 50 mg γ-globulin from rabbit no. 50 after third course of intravenous injection with killed pneumococcus', fig. 3
  4. (327/55) 'Fractionation of about 50 mg γ-globulin from rabbit no. 50 after second course of intravenous injection with killed pneumococcus', fig. 2
  5. (328/55) 'Fractionation of about 50 mg γ-globulin from rabbit no. 50 after first course of intravenous injections with killed pneumococcus', fig. 1
  6. (329/55) 'Fractionation of about 50 mg γ-globulin from rabbit no. 50 after fifth course of intravenous injection with killed pneumococcus', fig. 4
  7. (330/55) 'Fractionation of about 50 mg γ-globulin from rabbits after second course of intravenous injections with influenza virus type A', fig. 6
  8. (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
  9. (332/55) 'Fractionation of about 50 mg γ-globulin from rabbit one month after intramuscular injection of ovalbumin and adjuvant', fig. 8
  10. (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:
  1. (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.
  2. (381/56) 'Table 1. N-terminal amino acids of Bovine γ-Globulin'; see slide NY-1 below.
  3. (386/56) Partition 'Chromatography of bovine γ-globulin', fig. 1, re-run fractions run true; see slides 439/54 and 714/58.
  4. (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]:
  1. (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.
  2. (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)
  3. (480/56) 'Purification of inhibitor', shortened version of scheme 1, purification of fragment
  4. (481/56) 'Amino acid analysis', table 1, amino acid analysis of fragment and bovine serum albumin

Dates

  • 1954-1956

Extent

27 items

Shelfmark

MS. Photogr. e. 66

Repository Details

Part of the Bodleian Libraries Repository

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