人血浆极低密度载脂蛋白C-II的一级结构
Primary structure of very low density apolipoprotein C-II of human plasma.
作者信息
Jackson R L, Baker H N, Gilliam E B, Gotto A M
出版信息
Proc Natl Acad Sci U S A. 1977 May;74(5):1942-5. doi: 10.1073/pnas.74.5.1942.
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.
摘要
载脂蛋白C-II（apoC-II）是人类血浆极低密度脂蛋白的一种蛋白质成分，也是脂蛋白脂肪酶的激活蛋白，已被分离出来并对其氨基酸序列进行了研究。该蛋白质有78个氨基酸残基，不含半胱氨酸、胱氨酸和组氨酸。在25%甲酸中，用Bio-Gel P-30对apoC-II的溴化氰消化产物进行色谱分析，得到三个片段，分别命名为CNBr-I、-II和-III。它们分别含有50、19和9个残基。通过对完整蛋白质的胰蛋白酶肽段进行分离和测序，确定溴化氰片段的排列顺序为CNBr-III-I-II。胰蛋白酶肽段和CNBr肽段的氨基酸序列采用常规方法测定。根据这些信息，得以确定apoC-II的完整氨基酸序列。
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