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 YAMADA, K.
Right arrow Articles by ASAI, H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by YAMADA, K.
Right arrow Articles by ASAI, H.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 1982, Vol. 91, No. 4 1187-1195
© 1982 Japanese Biochemical Society

research-article

Extraction and Some Properties of the Proteins, Spastin B, from the Spasmoneme of Carchesium polypinum1

Kurumi YAMADA and Hiroshi ASAI

Department of Physics, School of Science and Engineering, Waseda University Shinjuku-ku, Tokyo 160

Proteins of the contractile spasmoneme from Carchesium polypinum were extracted in 2% SDS, 30% acetic acid, or 8 M urea. The proteins extracted in SDS had a wide molecular weight distribution when examined by SDS-polyacrylamide gel electrophoresis. On the other hand, the proteins extracted in urea and acetic acid had three major peaks with molecular weights of about 16,000, 18,000, and 22,000. Most of these proteins were soluble even in the absence of urea and furthermore were found to be monomeric, since the sedimentation coefficient, S20,w, measured by analytical ultracentrifugation was 2.0S. The electrophoretic mobility of the proteins extracted in urea or in acetic acid was examined on alkaline gels. In the presence of free Ca2+, the mobility was significantly reduced compared with that in the absence of free Ca2+. These Ca-binding proteins were heat-stable and could not interact with troponin I. The implications of these proteins and others in relation to the contractility of the spasmoneme in Carchesium stalk are discussed.

1This work was supported by Grants-in-Aid from the Yamada Science Foundation and the Ministry of Education, Science and Culture of Japan.


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 BiochemHome page
T. Itabashi, T. Terasaki, and H. Asai
Novel Nuclear and Cytoplasmic Proteins Detected by Anti-Zoothamnium arbuscula (Protozoa) Spasmin 1 Antibody in Mammalian Cells Are Dependent on the Cell Cycle
J. Biochem., November 1, 2004; 136(5): 651 - 657.
[Abstract] [Full Text] [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.