ISOLATION OF THE ALPHA-3-CHAIN OF HUMAN TYPE-V COLLAGEN AND CHARACTERIZATION BY PARTIAL SEQUENCING

被引：17
|
作者：
MANN, K
机构：
[1] Max-Planck-Institut für Biochemie
来源：
BIOLOGICAL CHEMISTRY HOPPE-SEYLER | 1992年 / 373卷 / 02期
关键词：
TYPE-V COLLAGEN; ALPHA-3-CHAIN; LYSYL ENDOPEPTIDASE; PARTIAL SEQUENCE ANALYSIS;
D O I：
10.1515/bchm3.1992.373.1.69
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The alpha-1-alpha-2-alpha-3-chain form of human type V collagen was solubilized from placenta by pepsin treatment and isolated by ion-exchange chromatography. The alpha-3-chain was further separated after denaturation of the triple helix also by ion-exchange chromatography, cleaved with lysyl endopeptidase and the fragments separated by size-exclusion chromatography and reversed phase HPLC. N-Terminal sequence analysis of the fragments and comparison to sequences contained in a database indicated a relatively high similarity of the alpha-3(V)-chain to alpha-1(V) and alpha-1(XI) with an identity of approximately 73%.
引用
收藏
页码：69 / 75
页数：7
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