By G. E. W. Wolstenholme
Chapter 1 Chairman's starting feedback (pages 1–3): C. Promageot
Chapter 2 the significance and Use of compatible Fractionation strategies 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 identity and Estimation of the Amide and C?Terminal Residues in Insulin by way of relief of the Ester with Lithium Borohydride (pages 70–81): A. C Chirnall and M. W. Rees
Chapter eight id of C?End teams in Proteins through 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 learn 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): okay. 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 id of Peptides in Partial Hydrolysates of Gelatin (pages 184–194): W. A. Schroeder
Chapter 18 Electron Optical and Chemical reports at the constitution of Collagen (pages 195–212): W. Grassmann
Chapter 19 Chairman's last feedback (pages 213–218): C. Fromageot
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Additional info for Ciba Foundation Symposium - The Chemical Structure of Proteins
Column made with 6 g. silane-treated silica in tube 1 . 1 cm. int. diam. When this was collected and tested by the liver slice assay method of Sutherland and Cori H. R. POILTER 38 (1948), it was found to show marked activity at 1 or 2 pg. while the insulin peak was essentially free of activity. Crude insulin supplied by Eli Lilly similarly showed the presence of this glucagon peak. When assayed carefully at Louvain by Professor C. de Duve and Dr. C. Vuylsteke, this glucagon proved to be nearly twice as active as a sample prepared from alkali-inactivated insulin by the method of Sutherland FIG.
Gorini in our laboratory has shown that the stability t o heat denaturation, for instance, w a s improved by metals such as manganese or calcium, and perhaps the metal which protects against heat would also show protection against adsorption a t the interface. PORTER: That is quite likely. LENS: Many insulins contain not only glucagon, but also a proteolytic enzyme which can hydrolyse protamine. It isn’t trypsin or trypsinogen. Have you done any work on this, Dr. Porter? PORTER:A sample which contains this enzyme has been run on the column and I am still waiting for the results.
PEDERSEY, K. , and SYNGE, R. L. &I. (1948). Acta clzem. , 2, 408. , and FRANKEL, S. (1949). , 9, 643. RYDON, H. , and SMITH, P. W.