Isolation of the native form of chicken gizzard myosin light-chain kinase.
作者： P K Ngai , C A Carruthers , M P Walsh
DOI: 10.1042/BJ2180863
关键词:
摘要: A simple and rapid procedure for the purification of native form chicken gizzard myosin light-chain kinase (Mr 136000) is described which eliminates problems proteolysis previously encountered. During this procedure, a calmodulin-binding protein Mr 141000, co-purified with kinase, removed shown to be distinct on basis lack activity, different chymotryptic peptide maps, cross-reactivity monoclonal antibody turkey phosphorylation by purified catalytic subunit cyclic AMP-dependent kinase. This Mr-141000 identified as caldesmon Ca2+-dependent interaction calmodulin, Mr, Ca2+-independent skeletal-muscle F-actin, competition between calmodulin F-actin caldesmon, tissue content.
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