Identification of a major bovine heart Ca2+ binding protein.
The 100,000 x g supernatant of bovine heart has been chromatographed on DEAE-cellulose and the resultant fractions have been analyzed for both calcium binding activity and calmodulin activity. Of the four peaks of calcium binding activity detected by this procedure only a single peak (peak IV) was identified as calmodulin. The calcium binding activity of the largest peak (peak III) has been subjected to further purification and a single calcium binding protein of Mr 63,000 isolated. Biochemical and immunological results documented that the 63 kDa protein is identical to calregulin. The results of this study identify calregulin as a major bovine heart calcium binding protein.
D000818:Animals; D002135:Calcium-Binding Proteins / Q000302:isolation & purification*; D037282:Calreticulin; D002417:Cattle; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D008970:Molecular Weight; D009206:Myocardium / Q000737:chemistry*; D012261:Ribonucleoproteins / Q000302:isolation & purification*
D002135:Calcium-Binding Proteins; D037282:Calreticulin; D012261:Ribonucleoproteins