Skip Navigation

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 Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by SHIMIZU, N.
Right arrow Articles by OBINATA, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by SHIMIZU, N.
Right arrow Articles by OBINATA, T.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 1986, Vol. 99, No. 3 751-759
© 1986 Japanese Biochemical Society


other

Actin Concentration and Monomer-Polymer Ratio in Developing Chicken Skeletal Muscle1

Noriko SHIMIZU2 and Takashi OBINATA3

Department of Biology, Faculty of Science, Chiba University Yayoi-cho, Chiba, Chiba-260

3 To whom all correspondence should be addressed

The actin concentration and monomer-polymer ratio in developing chicken skeletal muscle were determined by means of a DNase I inhibition assay. The concentration of G-actin in embryonic muscle was much higher than the critical concentration for polymerization of purified actin. As muscle development progressed, the amount of total actin remarkably increased, whereas the concentration of G-actin markedly decreased, and finally in adults reached the critical concentration for polymerization of purified actin. When the monomeric actin in the soluble fraction of embryonic muscle was purified, the critical concentration for polymerization of the embryonic actin decreased to the same value as that of adult skeletal muscle actin. On the other hand, there was no difference between the crude and purified actin in the type of actin. They consisted of {alpha}-, ß-, and {gamma}-actins; their amounts were in the order, ß>{gamma}>{alpha}. Furthermore, polymerization of the monomeric actin in the soluble fraction of embryonic muscle was induced by the addition of myosin or HMM. The large amount of monomeric actin in the embryonic skeletal muscle may be due to the presence of some factor(s) which inhibits actin polymerization and also to an insufficiency of myosin.

1 This study was supported in part by research grants from the Ministry of Education, Science and Culture, the National Center for Nervous, Mental and Muscular Disorders (NCNMMD) of the Ministry of Health and Welfare of Japan, and the Muscular Dystrophy Association of America (MDA).

2 Present address: Department of Medicine, Pharmacological and Physiological Sciences, The University of Chicago, Chicago, Illinois 60637.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
J. Cell Sci.Home page
S. Yamashiro, E. A. Cox, D. L. Baillie, J. D. Hardin, and S. Ono
Sarcomeric actin organization is synergistically promoted by tropomodulin, ADF/cofilin, AIP1 and profilin in C. elegans
J. Cell Sci., December 1, 2008; 121(23): 3867 - 3877.
[Abstract] [Full Text] [PDF]


Home page
JCBHome page
S. Ono, D. L. Baillie, and G. M. Benian
UNC-60B, an ADF/Cofilin Family Protein, Is Required for Proper Assembly of Actin into Myofibrils in Caenorhabditis elegans Body Wall Muscle
J. Cell Biol., May 3, 1999; 145(3): 491 - 502.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. Ono and G. M. Benian
Two Caenorhabditis elegans Actin Depolymerizing Factor/Cofilin Proteins, Encoded by the unc-60 Gene, Differentially Regulate Actin Filament Dynamics
J. Biol. Chem., February 6, 1998; 273(6): 3778 - 3783.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
L. S. Minamide, W. B. Painter, G. Schevzov, P. Gunning, and J. R. Bamburg
Differential Regulation of Actin Depolymerizing Factor and Cofilin in Response to Alterations in the Actin Monomer Pool
J. Biol. Chem., March 28, 1997; 272(13): 8303 - 8309.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
R Nagaoka, K Kusano, H Abe, and T Obinata
Effects of cofilin on actin filamentous structures in cultured muscle cells. Intracellular regulation of cofilin action
J. Cell Sci., January 2, 1995; 108(2): 581 - 593.
[Abstract] [PDF]



Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.