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

J. Biochem, 1987, Vol. 101, No. 4 889-895
© 1987 Japanese Biochemical Society

other

E-F Hand Structure-Domain of Calcium-Activated Neutral Protease (CANP) Can Bind Ca2+ Ions1

Yasufumi MINAMI, Yasufumi EMORI, Hiroshi KAWASAKI and Koichi SUZUKI

Department of Molecular Biology, The Tokyo Metropolitan Institute of Medical Science Bunkyo-ku, Tokyo 113

The cDNA fragments corresponding to the domains with four consecutive E-F hand structures in the large and small subunits of chicken and rabbit calcium-activated neutral protease (CANP) were inserted into an expression vector (pUC8 or pUC18). The resulting plasmids were used to transform E. coli, and isopropyl-1-thio-ß-D-galactoside (IPTG)-inducible expression was performed. The resulting four kinds of E-F hand structure-domains (the chicken large subunit, rabbit high- and low-calcium-requiring large subunits, and rabbit small subunit) were purified and analyzed for their calcium-binding abilities and capacities by the microscale filter assay. Most of the E-F hand structures could bind calcium and 2 or 4 mol of Ca2+ ions bound to the four consecutive E-F hand structures. The calcium-binding affinity of the E-F hand structures in the large subunit roughly corresponds to the calcium concentration required for its CANP activity.

1This study was supported in part by Grants-in-Aid for Scientific Research from 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. Biol. Chem.Home page
B. Chagot, F. Potet, J. R. Balser, and W. J. Chazin
Solution NMR Structure of the C-terminal EF-hand Domain of Human Cardiac Sodium Channel NaV1.5
J. Biol. Chem., March 6, 2009; 284(10): 6436 - 6445.
[Abstract] [Full Text] [PDF]

Home page
 J BiochemHome page
M. W. Park and Y. Emori
Drosophila Calpain B is Monomeric and Autolyzes Intramolecularly
J. Biochem., February 1, 2008; 143(2): 217 - 228.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
D. Guerini, B. Pan, and E. Carafoli
Expression, Purification, and Characterization of Isoform 1 of the Plasma Membrane Ca2+ Pump: FOCUS ON CALPAIN SENSITIVITY
J. Biol. Chem., October 3, 2003; 278(40): 38141 - 38148.
[Abstract] [Full Text] [PDF]

Home page
 Physiol. Rev.Home page
D. E. GOLL, V. F. THOMPSON, H. LI, W. WEI, and J. CONG
The Calpain System
Physiol Rev, July 1, 2003; 83(3): 731 - 801.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
R. P. Guttmann and G. V. W. Johnson
Oxidative Stress Inhibits Calpain Activity in Situ
J. Biol. Chem., May 22, 1998; 273(21): 13331 - 13338.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. S. Elce, C. Hegadorn, and J. S. C. Arthur
Autolysis, Ca2+ Requirement, and Heterodimer Stability in m-Calpain
J. Biol. Chem., April 25, 1997; 272(17): 11268 - 11275.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Molinari, M. Maki, and E. Carafoli
Purification of µ-Calpain by a Novel Affinity Chromatography Approach
J. Biol. Chem., June 16, 1995; 270(24): 14576 - 14581.
[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.