Chromatographic purification of soluble elastin.
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.
Abraham
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Department of Pathology, University of California, School of Medicine, Los Angeles 90024, USA.
Carnes
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WH
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001011:Aorta / Q000737:chemistry; D002847:Chromatography, Agarose; D002848:Chromatography, DEAE-Cellulose; D003300:Copper / Q000172:deficiency; D004549:Elastin / Q000737:chemistry / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D012995:Solubility; D013552:Swine; D014508:Urea
D000596:Amino Acids; D003300:Copper; D014508:Urea; D004549:Elastin