Primary structure of very low density apolipoprotein C-II of human plasma.
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Jackson RL, Baker HN, Gilliam EB, Gotto AM Jr
Primary structure of very low density apolipoprotein C-II of human plasma.
Proc Natl Acad Sci U S A. 1977 May;74(5):1942-5.
- PubMed ID
- 194244 [ View in PubMed]
- Abstract
Apolipoprotein C-II (apoC-II), a protein constituent of very low density lipoproteins of human plasma and the activator protein of lipoprotein lipase, has been isolated and its amino acid sequence has been 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 CNBr-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.