Abstract
Summary and Conclusions
A method has been developed for the purification of a 27,000 MW CaBP from human renal necropsy specimens. The purification was attained by application of DEAE-cellulose chromatography, gel filtration chromatography, and preparative acrylamide gel electrophoresis. The method yields a protein which migrates as a single band on acrylamide gel electrophoresis and has a specific calcium binding activity 184-fold greater than that of human albumin fraction V.
The authors acknowledge the cooperation of the Department of Pathology, Fitzsimons Army Medical Center, in providing necropsy specimens in support of this research.
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