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Group B - slides relating to other proteins or techniques used in protein chemistry, 1952-1959

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MS. Photogr. e. 69

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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'

Dates

  • 1952-1959

Extent

28 items

Shelfmark

MS. Photogr. e. 69

Repository Details

Part of the Bodleian Libraries Repository

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Weston Library
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