The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
STUDIES ON EGG YOLK PROTEINS
V. ELECTROPHORETIC AND ULTRACENTRIFUGAL INVESTIGATIONS ON THE HOMOGENEITIES AND SOME PROPERTIES OF α- AND β-LIPOVITELLIN
HIROSHI SUGANO
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1959 Volume 46 Issue 4 Pages 417-424

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Abstract

1. Both α- and β-lipovitellin were homogeneous elect rophoretically in the pH range 6.8 to 9.9 and 4.9 to 10.5, respectively, whereas at pH 4.2 both were heterogeneous. Ultracentrifugal analysis at pH 9.8 and μ 0.15 indicated the heterogeneities of both preparations.
2. From the mobility curve, the isoelectric point of β-lipovitellin was pH 5.9 at an ionic strength of 0.30.
3. From the variation of mobility of β-lipovitellin with buffer composi-tion, it was pointed out that the divalent anions such as carbonate and sulfate had the binding ability to β-lipovitellin, but not monovalent ions such as ammonium and chloride.
4. The mobility of β-lipovitellin depended on the inoic strength of buffer. There was a marked decrease in the mobility of β-lipovitellin with increase in ionic strength.
5. Some informations on the solubility property of β-lipovitellin in the pH range from 4.0 to 10.0 were obtained.

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© The Japanese Biochemical Society
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