By G. E. W. Wolstenholme
Chapter 1 Chairman's beginning feedback (pages 1–3): C. Promageot
Chapter 2 the significance and Use of appropriate Fractionation systems for Structural experiences 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 standard 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 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 yes 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 id 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 ultimate feedback (pages 213–218): C. Fromageot
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Additional info for Ciba Foundation Symposium - The Chemical Structure of Proteins
Phase diagram of the system SaH,PO,, water and ethyl cellosolve a t 18' Arrow indicates position of plait point. (Figs. 1-31, 5-8 from Binchern. 2. '2;" 33 P A R T I T I O S CHROMSTOGRAPHY O F P R O T E I N S which it has been used successfully is ethyleneglycol monobutyl ether (butyl cellosolve). All systems involving this solvent are temperature-labile, and it is essential that the temperature be controlled within 1 or 2", thus considerably increasing the work required to establish partition coefficients and run columns.
You are in a much stronger position, in considering the symmetry of your curves. I n the chromatographic method slight distortion of the curve can arise from poor packing. It has to be repeated a t least three or four times to be quite sure that any slight asymmetries are significant. It is quite possible that the resolving power is less and the secondary component is separated. CRAIG: It may be just a question of selectivity for that particular component. The distribution may be more selective for these two, but it’s quite possible that it could be less selective for some other component in the series.
On this account chromatography of whole egg white was undertaken (Tallan and Stein, 1951) to ascertain the behaviour of native lysozyme. The results are shown in Fig. 5 . Much ninhydrin-positive material is present, including a large peak a t the column volume that probably contains the bulk of the egg white proteins. Oiily one peak exhibiting lytic activity can be detected, however, the position of which corresponds exactly to that of peak A in Fig. 4. I n fact, when isolated lysozyme is added t o egg white prior t o chromatography, the activity peak shown in Fig.