Reactivation of lipid-depleted Ca2+-ATPase by a nonionic detergent.
作者： W L Dean , C Tanford
DOI: 10.1016/S0021-9258(17)40426-1
关键词:
摘要: The Ca2+-ATPase of sarcoplasmic reticulum can be reversibly delipidated by precipitation with polyethyleneglycol in the presence deoxycholate and glycerol to as low 4 mol phospholipid/mol enzyme polypeptide then reactivated 90% its original ATPase activity addition phosphatidylcholine. Furthermore, preparation exhibits nearly same if nonionic detergent dodecyl octaoxyethyleneglycol monoether is substituted for added phospholipid. soluble retains several days. This first report retaining high less than about 30 phospholipid bound per polypeptide.
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