Chromatographic purification of soluble elastin.
作者信息
Abraham P A, Carnes W H
机构信息
Department of Pathology, University of California, School of Medicine, Los Angeles 90024, USA.
出版信息
Anal Biochem. 1978 Nov;91(1):115-22. doi: 10.1016/0003-2697(78)90821-7.
An improved method for extraction and purification of soluble elastin from aortas of copper-deficient swine has been devised. It depends upon the use of both acidic and neutral protease inhibitors during preparation. Collagen is first precipitated with acetic acid. A two-step separation and purification of elastin from the collagen-free extract is based on absorption of the acidic proteins on DEAE-cellulose and gel filtration through agarose. The protein recovered is homogeneous by gel electrophoresis. It has the molecular weight (75,000) and amino acid composition of the soluble elastin from the same source prepared by repeated coacervation.
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