Chick 28,000 Mr vitamin D-dependent calcium-binding protein in intestine, kidney and cerebellum. Purification using chromatofocusing.
A purification method has been developed for chick 28,000 Mr vitamin D-dependent calcium-binding protein, involving Blue Sepharose CL-6B column chromatography, heat treatment and chromatofocusing with a microparticulate anion exchanger (Mono P). It allowed the rapid and reproducible purification of milligram amounts of homogeneous calcium-binding protein with good yields from chick intestine, kidney and cerebellum. The calcium-binding proteins thus obtained have the same molecular weight of 28,000, heat stability, calcium binding capability and apparent isoelectric point of 4.0. These physico-chemical properties are in good agreement with those of proteins isolated by a previous procedure, which gave a low and variable yield of calcium-binding protein.
Okano
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Department of Hygienic Sciences, Kobe Women's College of Pharmacy, Japan.
Lawson
D E
DE
D000818:Animals; D002531:Cerebellum / Q000032:analysis*; D002645:Chickens; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D015151:Immunoblotting; D007422:Intestines / Q000032:analysis*; D007525:Isoelectric Focusing; D007668:Kidney / Q000032:analysis*; D064030:S100 Calcium Binding Protein G / Q000302:isolation & purification*; D014020:Tissue Extracts / Q000032:analysis
D064030:S100 Calcium Binding Protein G; D014020:Tissue Extracts