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 KOBAYASHI, R.
Right arrow Articles by TASHIMA, Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by KOBAYASHI, R.
Right arrow Articles by TASHIMA, Y.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 1983, Vol. 94, No. 1 171-179
© 1983 Japanese Biochemical Society

research-article

Purification and Some Properties of Porcine Kidney Tropomyosin

Ryoji KOBAYASHI*,1, Yoshiaki NONOMURA**, Akira OKANO*** and Yohtalou TASHIMA*

*Department of Biochemistry, Akita University School of Medicine Akita 010
**Department of Pharmacology, The University of Tokyo Hongo, Bunkyo-ku, Tokyo 113
***Department of Biochemistry, Institute of Adaptation Medicine, Shinshu University School of Medicine Matsumoto, Nagano 390

1To whom all correspondence and reprint requests should be addressed.

A tropomyosin has been purified from porcine kidney and its properties compared with those of rabbit skeletal muscle tropomyosin. Kidney tropomyosin was separated from contaminating vascular smooth muscle tropomyosin by hydroxylapatite chromatography. Kidney tropomyosin resembles tropomyosin from other non-muscle cells in regard to subunit size, mobility on SDS-polyacrylamide gels in the presence and absence of 6 m urea, amino acid composition and morphology. The binding of tropomyosin to F-actin is strongly dependent on the Mg2+ concentration. With kidney tropomyosin, binding begins at 1 min Mg2+ and is complete at about 4–5 mM, while with muscle tropomyosin, binding is initiated at 1 mM Mg2+ and reaches saturation at 2–3 mM Mg2+. Both kidney and muscle tropomyosins bind to actin in a similar ratio of 1 tropomyosin/6–7 actin monomers at saturation. Both kidney and skeletal muscle tropomyosins prevent "severing" of F-actin filaments induced by gelsolin/villin-like protein purified from kidney. These results suggest that, in non-muscle cells, tropomyosin may protect microfilaments from Ca2+-dependent solation at the site where they may interact with myosin.


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




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.