By Hans Neurath (Eds.)

The Proteins Chemistry, organic task, and techniques V2A.

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8). While not enough of the topography of the protein molecule is known to explain these phenomena in detail, it would appear to the author that the general features are interpretable in terms of competitive interactions with charged groups of different hydration energies in regions of widely varying dielectric constant. It seems important to stress competitive interactions since in aqueous solution all of the valencies of atoms or radicals may be considered saturated with solvent, if not with another grouping, and the driving force for some reactions may be the relative affinity for solvent molecules of the groups involved.

1 86 This air-oxidation appears to affect first the traces of carotenoids present and eventually the unsaturated fatty acid esters. 6). Instability also appeared during attempts to measure the colloid osmotic pressure of this protein: high, unstable values indicating dis­ sociation of the lipoprotein. 61 Similar difficulties were met with Mache(186) G. S. A d a i r a n d Μ . E . A d a i r [/. Physiol 1 0 2 , 17 ( 1 9 4 3 ) ] , h a v e p r e p a r e d a crude l i p o p r o t e i n fraction, p r o b a b l y B i , b y p r e c i p i t a t i o n b e t w e e n 5 0 a n d 6 0 per c e n t s a t u r a t e d (NHO2SO4.

A . R i e h e r t , J. W . C a m e r o n , a n d P . M . , J. Am. Chem. Soc. 7 1 , 5 4 1 ( 1 9 4 9 ) . Biol. Chem. 1 3 7 , 4 8 5 ( 1 9 4 1 ) . (178) G. Blix, A. T i s e l i u s , a n d H . 7 per c e n t p h o s p h o l i p i d e if all t h e p h o s p h o r u s w a s from t h i s source. O n l y a b o u t h a l f t h i s a m o u n t w a s f o u n d i n l i p i d e e x t r a c t s , h o w e v e r . A f a t t y a c i d d e t e r ­ m i n a t i o n i n d i c a t e d t h a t 2 0 . 4 per c e n t of t h e l i p o p r o t e i n w a s f a t t y a c i d .

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