Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Suzuki, R.
Right arrow Articles by Morita, F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Suzuki, R.
Right arrow Articles by Morita, F.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J. Biol. Chem., Vol. 262, Issue 24, 11410-11412, 08, 1987

F-actin-binding synthetic heptapeptide having the amino acid sequence around the SH1 cysteinyl residue of myosin

R Suzuki, N Nishi, S Tokura and F Morita

The heptapeptide Ile-Arg-Ile-Cys-Arg-Lys-Gly-ethyl ester, having the amino acid sequence around the SH1 of myosin heavy chain, was coprecipitated with F-actin after ultracentrifugation. The heptapeptide inhibited the formation of acto-S-1 rigor complex by competing with S-1 for actin. Assuming a simple competitive inhibition, the dissociation constant of acto-heptapeptide complex was evaluated as 0.23 mM. An N- terminal tripeptide derivative from the heptapeptide Ile-Arg-Ile-methyl ester also formed a complex with F-actin with a dissociation constant of 1.1 mM. However, the other piece, Cys-Arg-Lys-Gly-ethyl ester, and a tetrapeptide, Val-Leu-Glu-Gly-ethyl ester, having the sequence adjacent to the N-terminal of the heptapeptide, scarcely bound with F-actin. These results suggest that part of the actin-binding site of myosin heavy chain around SH1 (Katoh, T., Katoh, H., and Morita, F. (1985) J. Biol. Chem. 260, 6723-6727) has the sequence of Ile-Arg-Ile and it is located adjacent to SH1 on its N-terminal side.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
Am. J. Physiol. Heart Circ. Physiol.Home page
X. Chen, K. Pavlish, and J. N. Benoit
Myosin phosphorylation triggers actin polymerization in vascular smooth muscle
Am J Physiol Heart Circ Physiol, November 1, 2008; 295(5): H2172 - H2177.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
E.-K. Lim, M. R. Roberts, and D. J. Bowles
Biochemical Characterization of Tomato Annexin p35. INDEPENDENCE OF CALCIUM BINDING AND PHOSPHATASE ACTIVITIES
J. Biol. Chem., December 25, 1998; 273(52): 34920 - 34925.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
J. R. Sims, S. Karp, and D. E. Ingber
Altering the cellular mechanical force balance results in integrated changes in cell, cytoskeletal and nuclear shape
J. Cell Sci., December 1, 1992; 103(4): 1215 - 1222.
[Abstract] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1987 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement