Document Detail


Effect of avidin binding to SH1 on the interface between subfragment-1 and F-actin.
MedLine Citation:
PMID:  3584099     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The subfragment-1-avidin complex, in which avidin is attached to a well defined thiol group called SH1, was purified by CM cellulose column chromatography or affinity chromatography using lipoic acid agarose. The interaction of the purified complex with F-actin was compared to that of normal subfragment-1 using chemical cross-linking and limited tryptic digestion techniques. It was found that the binding of avidin to SH1 lowered the extent of cross-linking between the subfragment-1 heavy chain and actin. The amount of the 175K product decreased to about 50% of the normal level and that of the 165K product decreased to about 35%. It was also found that the binding of avidin abolished the protective effect of F-actin on the 50K-22K junction of the S-1 heavy chain against tryptic attack. Since more than 95% of the S-1-avidin complex was attached to F-actin under our experimental conditions, these changes are due to an alteration of the S-1-actin interface. Considering the facts that SH1 is located on the side of S-1 facing the F-actin, in the tertiary structure, and is close to the cross-linked site and to the 50K-22K junction, in the primary structure, it is quite likely that avidin bound to SH1 causes these effects by sterically preventing the close contact of S-1 and actin.
Authors:
K Yamamoto; T Sekine
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of biochemistry     Volume:  101     ISSN:  0021-924X     ISO Abbreviation:  J. Biochem.     Publication Date:  1987 Feb 
Date Detail:
Created Date:  1987-07-06     Completed Date:  1987-07-06     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0376600     Medline TA:  J Biochem     Country:  JAPAN    
Other Details:
Languages:  eng     Pagination:  519-23     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Actins*
Avidin*
Binding Sites
Chromatography / methods
Cross-Linking Reagents
Myosin Subfragments
Myosins*
Peptide Fragments*
Protein Binding
Sulfhydryl Compounds*
Trypsin
Chemical
Reg. No./Substance:
0/Actins; 0/Cross-Linking Reagents; 0/Myosin Subfragments; 0/Peptide Fragments; 0/Sulfhydryl Compounds; 1405-69-2/Avidin; EC 3.4.21.4/Trypsin; EC 3.6.4.1/Myosins

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


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