Document Detail


Physicochemical properties of succinylated calfskin pepsin-solubilized collagen.
MedLine Citation:
PMID:  17690454     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Some physicochemical properties of calfskin pepsin-solubilized collagen (PSC) and succinylated PSC (SPSC) were compared. The amino acid profile remained significantly unchanged. Sodium dodecylsulphate-polyacrylamide gel electrophoresis showed that subunits of SPSC migrated less than those of PSC. The denaturation temperatures of PSC and SPSC were 38.4 degrees C and 34.7 degrees C respectively. Succinylation slightly altered the triple-helical conformation of collagen, as determined by circular dichroism.
Authors:
Zhongkai Zhang; Wentao Liu; Dong Li; Guoying Li
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2007-08-07
Journal Detail:
Title:  Bioscience, biotechnology, and biochemistry     Volume:  71     ISSN:  0916-8451     ISO Abbreviation:  Biosci. Biotechnol. Biochem.     Publication Date:  2007 Aug 
Date Detail:
Created Date:  2007-08-27     Completed Date:  2007-12-20     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9205717     Medline TA:  Biosci Biotechnol Biochem     Country:  Japan    
Other Details:
Languages:  eng     Pagination:  2057-60     Citation Subset:  IM    
Affiliation:
The Key Laboratory of Leather Chemistry and Engineering of the Ministry of Education, Sichuan University, Chengdu, PR China.
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MeSH Terms
Descriptor/Qualifier:
Animals
Cattle
Collagen / chemistry*,  metabolism
Electrophoresis, Polyacrylamide Gel
Pepsin A / metabolism
Protein Conformation
Protein Denaturation
Skin / chemistry*
Solubility
Succinates
Temperature
Chemical
Reg. No./Substance:
0/Succinates; 9007-34-5/Collagen; EC 3.4.23.1/Pepsin A

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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