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Ciba Foundation Symposium - Chemistry and Biology of by Gordon Ethelbert Ward Wolstenholme, Maeve O'Connor

By Gordon Ethelbert Ward Wolstenholme, Maeve O'Connor

Content:
Chapter 1 Chairman's commencing feedback (pages 1–3): W. T. J. Morgan
Chapter 2 common Chemistry of the Mucopolysaccharides (pages 4–21): M. Stacey
Chapter three Physicochemical stories on Hyaluronic Acids (pages 22–41): B. S. Blumberg and A. G. Ogston
Chapter four Immunochemical ways to Polysaccharide and Mucopolysaccharide constitution (pages 42–63): Elvina Kabat
Chapter five Biosynthesis of Mucopolysaccharides: The Uridine Nucleotides of team a Streptococci (pages 64–84): Albert Dorfman and J. Anthony Cifonelli
Chapter 6 Sulphated Galactosamine?Containing Mucopolysaccharides (pages 85–92): Roger W. Jeanloz, Pierre J. Stoffyn and Monique Tremege
Chapter 7 The Presence in Cartilage of a fancy Containing Chondroitin Sulphate mixed with a Non?Collagenous Protein (pages 93–115): S. M. Partridge and H. F. Davis
Chapter eight The impartial Heteropolysaccharides in Connective Tissue (pages 116–189): Z. Disch, A. Danilczenko and G. Zelmenis
Chapter nine N?Containing Saccharides in Human Milk (pages 140–156): Paul Lgyorgy
Chapter 10 The Pharmacological results of Polysaccharides (pages 157–186): Rolf Meier
Chapter eleven Mucopolysaccharides of Gram?Negative micro organism: more moderen Chemical and organic points (pages 187–199): Otto Westphal, Otto Luderitz, Erwin Eichenberger and Erwin Neter
Chapter 12 Mucopolysaccharides linked to Blood team Specificity (pages 200–215): W. T. J. Morgan
Chapter thirteen Blood crew lively elements of Plant starting place (pages 216–233): Georg F. Springer
Chapter 14 Mucopolysaccharides of Epithelial Mucus (pages 234–244): Lars Odin
Chapter 15 Glycoproteins of Plasma (pages 245–266): Richard J. Winzler
Chapter sixteen Colloidal houses of Urinary Mucopolysaccharides (pages 268–286): N. F. Maclaga and A. J. Anderso
Chapter 17 The Prosthetic workforce of a few Mucoproteins and its dating to Influenza Virus (pages 287–295): Alfred Gottschalk
Chapter 18 Neuraminic Acid (pages 296–313): E. Klenk

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Indeed, with antiserum 34)D,, the difference between 5 and 6 residues is only slightly greater than the experimental error. One would infer, therefore, that 6 glucose units should be fairly close to the upper limit in size for the antibody combining site. With respect to specificity of the combining site, the importance of the glucose configuration is illustrated by the substantially weaker inhibiting power of melibiose as compared with isomaltose, the only difference being the change in the OH on Ct4) of the non-reducing end of isomaltose from the glucose to the galactose configuration ; melibiose and rafinose are equally effective mole for mole.

Particle weight. The results are shown in Table I. Where several measurements have been made on material from the - 32 B. S. BLUMBERG AND A. G . OGSTON same source (as with umbilical cord and vitreous humour) the results are remarkably concordant. 5 x lo6; and the materials in sheep and ox synovial fluids differ markedly. The average particle weights of material in human synovial fluids vary from sample to sample: they fall within the same range as that of material from human umbilical cord, but differ from that of the ox synovial fluid complex.

1955b). Biochem. ,59, 626. LAURENT, T. C. (1955). J . b i d . , 216, 263. LAURENT, T. , and GERGELY, J. (1955). J. biol. , 212,325. , and JIALE,C. W. (1941). Biochem. ,35, 159. , and QUIBELL, T. 11. (19iO). Biochem. ,34, 625. MEYER,K. (1947). Physiol. , 27, 335. , and PALMER, J. VV. (1934). J. biol. , 107, 629. , SMYTII, E. , and DAWSON, & 13. I. (1939). J. bioZ. , 128, 319. MUIR,€1. (1956). Biochem. ,62, 26P. OGSTON, A. G. (1953). Trans. , 49, 1451. OGSTON, A. , and STANIER, J. E. (1950). Biochem.

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