Primary structure of very low density apolipoprotein C II of human plasma

R. L. Jackson, H. N. Baker, E. B. Gilliam, Antonio Gotto

Research output: Contribution to journalArticle

118 Scopus citations

Abstract

Apolipoprotein C-II (apoC-II), a protein constituent of very low density lipoproteins of human plasma and the activator protein of lipoprotein lipase, was isolated and its amino acid sequence studied. The protein has 78 amino acid residues and is lacking cysteine, cystine, and histidine. Chromatography on Bio-Gel P-30 in 25% formic acid of the cyanogen bromide digest of apoC-II yields three fragments designated as CNB-I, -II, and -III. They contained 50, 19, and 9 residues, respectively. The alignment of the cyanogen bromide fragments has been established as CNBr-III-I-II by isolation and sequence of the tryptic peptides of the intact protein. The amino acid sequences of the tryptic and CNBr peptides were determined by conventional methods. With this information, it was possible to establish the complete amino acid sequence of apoC-II.

Original languageEnglish (US)
Pages (from-to)1942-1945
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Volume74
Issue number5
DOIs
StatePublished - 1977

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'Primary structure of very low density apolipoprotein C II of human plasma'. Together they form a unique fingerprint.

Cite this