Download Ciba Foundation Symposium - The Chemical Structure of by G. E. W. Wolstenholme PDF

By G. E. W. Wolstenholme

Chapter 1 Chairman's starting feedback (pages 1–3): C. Promageot
Chapter 2 the significance and Use of appropriate Fractionation systems for Structural stories with Proteins (pages 4–16): Lyman C. Craig
Chapter three Chromatographic Purification of Ribonuclease and Lysozyme (pages 17–30): William H. Stein
Chapter four The Partition Chromatography of Proteins, with specific connection with Insulin and Glucagon (pages 31–42): R. R. Porter
Chapter five Peptides of normal Tissues (pages 43–57): R. L. M. Synge
Chapter 6 at the Terminal Residues of Chymotrypsinogen, Chymotrypsins, Trypsinogen and Trypsin (pages 58–69): P. Desnuelle and M. Rovery
Chapter 7 id and Estimation of the Amide and C?Terminal Residues in Insulin via relief of the Ester with Lithium Borohydride (pages 70–81): A. C Chirnall and M. W. Rees
Chapter eight identity of C?End teams in Proteins by way of relief with Lithium Aluminium Hydride (pages 82–97): Claude Fromageot and Marian Jutisz
Chapter nine Selective Cleavage of Peptides (pages 98–101): Pehr Edman
Chapter 10 Phenylisothiocyanate as a Reagent for the id of the Terminal Amino?Acids (pages 102–108): H. Fraenkel?Conrat
Chapter eleven Specificity of definite Peptidases and their Use within the research of Peptide and Protein constitution (pages 109–128): Emil L. Smith
Chapter 12 Acyl Migration within the examine of Protein constitution (pages 129–141): D. F. Elliott
Chapter thirteen Degradation of Peptides from the Amino finish (pages 142–145): F. Turba
Chapter 14 Degradation of Peptides from the Carboxyl finish (pages 146–150): T. Wieland
Chapter 15 Protamines and Nucleoprotamines (pages 151–164): ok. Felix
Chapter sixteen Fractionation of Pepsin?Catalysed Hydrolysates of Crystalbumin (pages 165–183): Paul Boulanger and Gerard Biserte
Chapter 17 a few Experiments at the Chromatographic Separation and identity of Peptides in Partial Hydrolysates of Gelatin (pages 184–194): W. A. Schroeder
Chapter 18 Electron Optical and Chemical reviews at the constitution of Collagen (pages 195–212): W. Grassmann
Chapter 19 Chairman's last comments (pages 213–218): C. Fromageot

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It will be very interesting to use this technique on other proteins of higher molecular weight. GRASSMAX:I should like to ask Dr. Smith about the quantitative estimation of proteins with the ninhydrin reaction. I would think that the reaction would be much less sensitive with proteins than with amino-acids and loner peptides, and I imagine that there would be difficulties with flocculation and so on. Are the extinction coefficients of different proteins the same or even similar? SMITH:At low concentrations of protein, flocculation does not appear t o be any problem.

2 M sodium phosphate buffer of pH 7 18 as eluant. atypical proteins, however. It remains to be seen whether a method more generally applicable to proteins as a class can be developed. REFERENCES FEVOLD, H. , and ALDERTON,G. (1949) in CARTER, H. , et al. Biochemical Preparations, 1, 67. HIRS,C. H. , and STEIX,W. H. (1953). J . biol. , 200, 493. KUNITZ,M. (1946). J . biol. , 164, 563. KUNITZ,M. (1948), in NORTHROP, J. , and HERRIOTT, R. M. Crystalline Enzymes. 2nd Ed. New York: Columbia Univ. Press.

C. (1952). Biochem. J . , 52, 87. OHIRA,T. (1939). J. agric. chern. Japan, 15, 370. Cited in Chew$. Abstr. (1939). 33, 6245. OHIRA,T. (1940a). J. agric. chem. Japan, 16, 1; B u l l . agric. chem. Japan, 16, 10. Cited in Chem. Abstr. (1940), 34, 3683. OHIRA,T. (1940b). J. agric. chem. Japan, 16, 293; Bull. agric. chem. Japan, 16, 71. Cited in Chem. Abstr. (1940), 34, 5826. PARK, J. T. J. b i d . , 194, 877. PARK, J. T. (19526). J. biol. , 194, 885. PARK, J. T. J. b i d . , 194, 897. PEDERSEY, K.

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