Abstract:
: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.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Waisman DM,Khanna NC,Tokuda Mdoi
10.1016/s0006-291x(86)80032-8subject
Has Abstractpub_date
1986-09-14 00:00:00pages
596-603issue
2eissn
0006-291Xissn
1090-2104pii
S0006-291X(86)80032-8journal_volume
139pub_type
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