文章基本信息

标题：Amino Acid Sequence of Human apoLp-Gln-II (apoA-II), an Apolipoprotein Isolated from the High-Density Lipoprotein Complex
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作者：H. B. Brewer ; S. E. Lux ; R. Ronan 等
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：1972
卷号：69
期号：5
页码：1304-1308
DOI：10.1073/pnas.69.5.1304
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：An apolipoprotein, designated by its carboxyl-terminal residue as apoLp-Gln-II, has been isolated from the human high-density lipoprotein family, and its complete aminoacid sequence was determined. The apoprotein, one of the two major apoproteins of this family, is composed of two identical polypeptide chains, each containing 77 amino acids. The two polypeptide chains are connected by a single disulfide bridge at position 6 in the sequence. The minimum molecular weight of the intact apoprotein is 17,380. The amino-terminal residue of each chain is pyrrolidone carboxylic acid, and the carboxyl-terminal residue is glutamine.
关键词：pyrrolidone carboxylic acid ; lipid-protein interactions ; human blood plasma ; automated Edman degradations ; protein structure