Extraction and Isolation of Type Ⅰ Ⅲ and Ⅴ Collagens and Their SDS-PAGE Analyses

Type Ⅰ Ⅲ and Ⅴ collagens were extracted from bovine dermis and cornea by using pepsin treatment in acetic acid solution, followed by salt precipitation and dialysis, to purify and isolate each type of collagens. The preparation process was analyzed by using sodium dodecyl sulfate polyacrylamide gel...

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Published inTransactions of Tianjin University Vol. 17; no. 2; pp. 111 - 117
Main Author 武继民 李志宏 袁晓燕 汪鹏飞 刘永清 王赫
Format Journal Article
LanguageEnglish
Published Heidelberg Tianjin University 01.04.2011
Tianjin Key Laboratory of Composite and Functional Materials, School of Materials Science and Engineering, Tianjin University, Tianjin 300072, China
Institute of Medical Equipment, Academy of Military Medical Sciences, Tianjin 300161, China%Institute of Medical Equipment, Academy of Military Medical Sciences, Tianjin 300161, China%Tianjin Key Laboratory of Composite and Functional Materials, School of Materials Science and Engineering, Tianjin University, Tianjin 300072, China
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ISSN1006-4982
1995-8196
DOI10.1007/s12209-011-1543-2

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Summary:Type Ⅰ Ⅲ and Ⅴ collagens were extracted from bovine dermis and cornea by using pepsin treatment in acetic acid solution, followed by salt precipitation and dialysis, to purify and isolate each type of collagens. The preparation process was analyzed by using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). A reducing agent, 2-mercaptoethanol, was used to remove disulfide bonds and analyze the structure of the bonds involved between α chains in some types of collagens. The use of delayed reducing methods resulted in the difference between α1 (Ⅲ) and α1 ( Ⅰ ) chains in a mixture containing type Ⅰ and Ⅲ collagens. The structure of disulfide bonds among α chains exists potentially in type V collagen prepared from the pepsin-treatment extraction at 4 ℃, which differs from type Ⅲ collagen in relation to the locations of disulfide bonds. Compared with pepsin-treated collagen at 4 ℃, the relative molecular weights of α1 (V) and α2 (V) chains treated at room temperature decrease by 4.6% and 6.0%, respectively. It is concluded that type Ⅰ Ⅲ and Ⅴ collagens can be prepared from bovine dermis and cornea by the use of pepsin treatment, salt precipitation and dialysis. The interchain disulfide bonds lie potentially near the edges of termini of type V collagen molecules in extracellular matrix, and a small number of interchain crosslinks exist in type V collagen.
Bibliography:SDS-PAGE
interchain
12-1248/T
TS59
collagen; interchain; SDS-PAGE; preparation; structure
S512.301
collagen
structure
preparation
ISSN:1006-4982
1995-8196
DOI:10.1007/s12209-011-1543-2