Electronic Resource
Springer
Cellular and molecular life sciences
3 (1947), S. 153-154
ISSN:
1420-9071
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Medicine
Notes:
Summary The electrophoretic patterns of normal casein (precipitated with acid from cow's milk) and of rennetcasein obtained in a veronal buffer at ap H of 7.3 are remarkably different from each other. The ascending boundary of the α-fraction of casein treated with rennet splits off into two peaks showing the presence of two subfractions (α1 and α2). The proportion of quantity of the faster (α1) and of the slower (α2) subfraction was found to be about 0.9:1. The α-component of casein which was not treated with active rennet behaved under the same conditions electrophoretically uniform.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF02137465
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