重组人组织因子的翻译后修饰

Post-translational modifications of recombinant human tissue factor.

作者信息

Paborsky L R, Harris R J

机构信息

Department of Cardiovascular Research, Genentech, Inc., South San Francisco, CA 94080.

出版信息

Thromb Res. 1990 Dec 1;60(5):367-76. doi: 10.1016/0049-3848(90)90219-3.

DOI:10.1016/0049-3848(90)90219-3

PMID:2084958

Abstract

Recombinant human tissue factor (rTF) purified from transfected mammalian cells is a glycoprotein that contains N-linked, but not O-linked oligosaccharides. Two of the three potential N-linked sites in the extracellular portion are fully glycosylated, while one site is approximately 90% utilized. These sites have complex-type oligosaccharides attached. The potential N-linked site in the cytoplasmic domain near the C-terminus is not glycosylated. Characterization of the tryptic map of rTF confirmed most of the proposed amino acid sequence. In addition, the disulfide bonds (between Cys-49 and Cys-57 and between Cys-186 and Cys-209) were demonstrated by FAB-MS analysis of cysteine-containing fragments obtained from the tryptic map.

摘要

从转染的哺乳动物细胞中纯化得到的重组人组织因子（rTF）是一种糖蛋白，含有N-连接型而非O-连接型寡糖。细胞外部分的三个潜在N-连接位点中有两个被完全糖基化，而一个位点的利用率约为90%。这些位点连接有复合型寡糖。靠近C端的细胞质结构域中的潜在N-连接位点未被糖基化。rTF胰蛋白酶图谱的表征证实了大部分推测的氨基酸序列。此外，通过对从胰蛋白酶图谱获得的含半胱氨酸片段进行FAB-MS分析，证实了（Cys-49与Cys-57之间以及Cys-186与Cys-209之间的）二硫键。