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  • 标题:Lipoprotein lipase cofactor activity of a carboxyl-terminal peptide of apolipoprotein C-II
  • 本地全文:下载
  • 作者:T A Musliner ; E C Church ; P N Herbert
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:1977
  • 卷号:74
  • 期号:12
  • 页码:5358-5362
  • DOI:10.1073/pnas.74.12.5358
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:Apolipoprotein C-II (apoC-II) is a small protein found associated with the plasma lipoproteins. It serves a unique function in the activation of the enzyme lipoprotein lipase (triacylglycerol acyl-hydrolase, EC 3.1.1.3 ). ApoC-II contains a single arginine residue, permitting tryptic cleavage into two peptides after succinylation of the native protein. The succinylated amino-terminal peptide, approximately 50 residues, did not activate lipoprotein lipase. The succinylated carboxyl-terminal peptide, about 29 residues, had significant cofactor activity. Relative to native apoC-II, the maximal activation observed with the succinylated carboxyl-terminal peptide was 50% lower and the concentration required for half-maximal activity was approximately 10 times higher. Mixtures of the carboxyl- and amino-terminal peptides had no more activity than the carboxyl-terminal peptide alone. Localization of functional properties to the carboxyl region is a feature also common to apolipoproteins C-III, A-II, and A-I.
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