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• W2069717269 endingPage "1945" @default.
• W2069717269 startingPage "1942" @default.
• W2069717269 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." @default.
• W2069717269 created "2016-06-24" @default.
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• W2069717269 date "1977-05-01" @default.
• W2069717269 modified "2023-10-12" @default.
• W2069717269 title "Primary structure of very low density apolipoprotein C-II of human plasma." @default.
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• W2069717269 doi "https://doi.org/10.1073/pnas.74.5.1942" @default.
• W2069717269 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/431048" @default.
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