By G. E. W. Wolstenholme
Chapter 1 Chairman's commencing feedback (pages 1–3): C. Promageot
Chapter 2 the significance and Use of appropriate Fractionation approaches for Structural reports 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 by means of aid 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 by means of aid 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 sure Peptidases and their Use within the learn 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 id of Peptides in Partial Hydrolysates of Gelatin (pages 184–194): W. A. Schroeder
Chapter 18 Electron Optical and Chemical stories at the constitution of Collagen (pages 195–212): W. Grassmann
Chapter 19 Chairman's remaining comments (pages 213–218): C. Fromageot
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Additional info for Ciba Foundation Symposium - The Chemical Structure of Proteins
ELLIOTT: I thought that the urea form might be component C. NEUBERGER: That could be easily checked-one could see whether on acid hydrolysis CO, is liberated. SMITH: Except that there is so much carbonate here anyhow. * PORTER: As regards the small component in the ribonuclease, we found that the main component had one lysine end-group, while the small component always had the same end-group, but only 1/10 t o 1/5 per mole of 13,000 or 14,000. We assumed that some slight contamination with the main peak was still occurring, but repeated attempts to free it from this trace end-group failed completely.
Difficulties of the method There are several intrinsic difficulties in this technique, notably the risk of denaturing the protein and the inability t o get sufficient protein into solution in the moving phase. Denaturation may be caused by the organic solvent or may follow adsorption a t one of the interfaces (liquid-liquid and liquid-solid) on the column. The denaturation caused by the organic solvent can in most cases be avoided by working a t low temperatures-as low as - 5 " has been used. I 34 R.
CHROMATOGRA4PHY O F RIBOSYCLEASE A S D LYSOZUME 21 If larger quantities of ribonuclease A are desired, it is more convenient to employ as starting material the crystalline preparations obtained by the Kunitz-McDonald (1948) procedure. In this case the effective load on the large columns can be much greater than that employed with crude extracts of pancreas. For example, starting with 750 mg. of crystalline material, it was possible to isolate 400 mg. of a product which Effluent volume, cc. 3. Chromatographic homogeneity of purified ribonuclease A prepared from crystalline ribonuclease (Kunitz) by cliromatography on a large scale.