Title : Retention of enzyme activity by detergent-solubilized sarcoplasmic Ca2+ -ATPase.

Pub. Date : 1976 Jun 1

PMID : 132186






2 Functional Relationships(s)
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1 Preliminary molecular weight measurements indicate that the Ca2+ -ATPase exists as an oligomer in the native membrane: fully active enzyme in Tween 80 has a minimal protein molecular weight of about 400 000, corresponding to a trimer or tetramer of the ATPase polypeptide chain, and even the inactive enzyme in deoxycholate contains a substantial fraction of dimeric protein. Polysorbates dynein axonemal heavy chain 8 Homo sapiens
2 Preliminary molecular weight measurements indicate that the Ca2+ -ATPase exists as an oligomer in the native membrane: fully active enzyme in Tween 80 has a minimal protein molecular weight of about 400 000, corresponding to a trimer or tetramer of the ATPase polypeptide chain, and even the inactive enzyme in deoxycholate contains a substantial fraction of dimeric protein. Polysorbates dynein axonemal heavy chain 8 Homo sapiens