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 Asano, T.
Right arrow Articles by Kato, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Asano, T.
Right arrow Articles by Kato, K.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 1988, Vol. 103, No. 6 950-953
© 1988 Japanese Biochemical Society

research-article

Immunoassay for the ß{gamma} Subunits of GTP-Binding Proteins and Their Regional Distribution in Bovine Brain1

Tomiko Asano, Nobuko Kamiya, Rika Morishita and Kanefusa Kato

Department of Biochemistry, Institute for Developmental Research Aichi Prefectural Colony, Kasugai, Aichi 480-03

Antibodies were raised in rabbits against the ß{gamma} subunits of bovine brain GTP-binding proteins, and were purified with a ß{gamma}-coupled Sepharose column. Purified antibodies reacted strongly with 36,000-dalton ß subunit and slightly with 35,000-dalton ß and {gamma} subunits, but not with other proteins in an immunoblot assay. Using these purified antibodies, a sensitive enzyme immunoassay method for the quantification of brain ß{gamma} was developed. The assay system consisted of polystyrene balls with immobilized antibody F(ab')2 fragments and the same antibody Fab' fragments labeled with ß-{gamma}-galactosidase from Escherichia coli. The minimum detection limit of the assay was 3 fmol, or 130 pg. Samples from various regions of bovine brain were solubilized with 2% sodium cholate and 1 M NaCl, and the concentrations of ß{gamma} were determined. The ß{gamma} were detected in all the regions, and the highest concentrations were observed in the cerebral cortex and nucleus caudatus. The concentrations of ß{gamma} were higher than those of {alpha} subunit of GTP-binding protein, Go, in all the regions.

1This work was supported in part by a Grant-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
T. Furukawa, R. Miura, Y. Mori, M. Strobeck, K. Suzuki, Y. Ogihara, T. Asano, R. Morishita, M. Hashii, H. Higashida, et al.
Differential Interactions of the C terminus and the Cytoplasmic I-II Loop of Neuronal Ca2+ Channels with G-protein alpha  and beta gamma Subunits. II. EVIDENCE FOR DIRECT BINDING
J. Biol. Chem., July 10, 1998; 273(28): 17595 - 17603.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
R. Morishita, H. Nakayama, T. Isobe, T. Matsuda, Y. Hashimoto, T. Okano, Y. Fukada, K. Mizuno, S. Ohno, O. Kozawa, et al.
Primary Structure of a [IMAGE] Subunit of G Protein, [IMAGE][IMAGE], and Its Phosphorylation by Protein Kinase C
J. Biol. Chem., December 8, 1995; 270(49): 29469 - 29475.
[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.