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Fractionation of bovine serum lipoproteins and their characterization by gradient gel electrophoresis

Published online by Cambridge University Press:  01 June 2009

P. E. Brumby  and
V. A. Welch
P. E. Brumby
Affiliation:
National Institute for Research in Dairying, Shinfield, Reading
V. A. Welch
Affiliation:
National Institute for Research in Dairying, Shinfield, Reading
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Summary

Bovine serum lipoproteins were fractionated by precipitation with dextran sulphate followed by ultracentrifugation and were examined by paper electrophoresis and by disk electophoresis in acrylamide gels. Gels containing concentration gradients of both sucrose and acrylamide gave better resolution of lipoproteins than did gels of uniform composition or gels with a concentration gradient of sucrose and a uniform concentration of acrylamide.

The densities of the lipoprotein classes isolated (listed in order of increasing mobility on electrophoresis in acrylamide gels) were as follows:

I, d < 1·019; II, 1·039 <d<1·050;

III, 1·019 <d<1·039; IVa and IVb, d > 1·050.

Lipoproteins of classes I, II and III were precipitated by dextran sulphate. On paper electrophoresis, lipoproteins of class II had β mobility and lipoproteins of classes IVa and IVb had α mobility. Lipoproteins of class I remained at the origin.

The lipoprotein classes of bovine sera resembled those of sheep and goat sera in that class IV predominated. In contrast, the sera of several non-ruminant species showed a predominance of lipoprotein classes of low electrophoretic mobility.

Type
Original Articles
Information
Journal of Dairy Research , Volume 37 , Issue 1 , February 1970 , pp. 121 - 128
Copyright
Copyright © Proprietors of Journal of Dairy Research 1970

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