spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

This Article
Right arrow Full Text (PDF)
Right arrow References
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 arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Terasaki, A. G.
Right arrow Articles by Ohashi, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Terasaki, A. G.
Right arrow Articles by Ohashi, K.
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   Add to Twitter  
What's this?

Journal of Cell Science, Vol 108, Issue 3 857-868, Copyright © 1995 by Company of Biologists

JOURNAL ARTICLES

A high molecular mass protein isolated from chicken gizzard: its localization at the dense plaques and dense bodies of smooth muscle and the Z-disks of skeletal muscle

AG Terasaki, H Nakagawa, E Kotani, H Mori and K Ohashi
Department of Biology, Faculty of Science, Chiba University, Japan.

We purified a 450 kDa protein from a low-salt alkaline extract of chicken gizzard smooth muscle. This high molecular mass protein could be extracted with the low-salt alkaline solution at 37 degrees C but not at 4 degrees C. The 450 kDa protein was isolated from the extract by ammonium sulfate fractionation and following sequential column chromatography using hydroxylapatite, DEAE-Cellulofine A-800m and phenyl-Sepharose CL-4B resins. The partially purified protein molecule resembled a flexible rod with a globular head and an irregular-shaped tail. Its length was approximately 300 nm. The nucleotide sequence of the partial cDNA encoding this protein was determined and analyzed with a data base. The analysis showed that the protein revealed significant homology with the rod region of chicken filamin (57% homology in amino acid sequence). Immunoblot analysis showed that an affinity-purified antibody reacted exclusively with the 450 kDa protein band of smooth, skeletal and cardiac muscle tissues. By indirect immunofluorescence microscopy, we examined the localization of the 450 kDa protein in smooth and skeletal muscle cells. The affinity-purified antibody against the 450 kDa protein stained the dense plaques and dense bodies of smooth muscle, the peripheral region of Z-disks and the subsarcolemmal region of skeletal muscle. Immunoelectron microscopy confirmed the localization of the 450 kDa protein at the peripheral regions of the actin anchoring structures mentioned above. Judging from its amino acid sequence, molecular size, molecular shape, immunological reactivity and localization in muscle cells, the 450 kDa protein seemed to be a new component associated with the actin-anchoring structures of muscle tissues.(ABSTRACT TRUNCATED AT 250 WORDS)
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   Add to Twitter Twitter    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
K. Tokuraku, K. Matsushima, T. Matui, H. Nakagawa, M. Katsuki, R. Majima, and S. Kotani
The Number of Repeat Sequences in Microtubule-associated Protein 4 Affects the Microtubule Surface Properties
J. Biol. Chem., August 8, 2003; 278(32): 29609 - 29618.
[Abstract] [Full Text] [PDF]


© The Company of Biologists Ltd 1995