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

J. Biochem, 1990, Vol. 108, No. 2 230-234
© 1990 Japanese Biochemical Society

research-article

Molecular Cloning and Sequencing of the cDNA of Rat {alpha}1-Protease Inhibitor and Its Expression in COS-1 Cells1

Yoshio Misumi, Miwa Sohda, Kumiko Ohkubo, Noboru Takami, Kimimitsu Oda and Yukio Ikehara2

Department of Biochemistry and Radioisotope Laboratory, Fukuoka Unwersity School of Medicine Jonan-ku, Fukuoka, Fukuoka 814-01

2To whom correspondence should be addressed

A cDNA clone for {alpha}1-protease inhibitor (pc{alpha}1PI212) was isolated from a {gamma}ZAP rat liver cDNA library. The 1.4 kb cDNA insert of pc{alpha}1PI212 contained an open reading frame that encodes a 411-residue polypeptide (48,125 Da), in which a signal peptide of 24 residues was identified by comparison with the NH2-terminal sequence of the purified protein. Three potential sites for N-linked glycosylation were found in the molecule, accounting for the difference in molecular mass between the predicted form and the purified protein (56 kDa). The deduced primary structure of rat {alpha}-protease inhibitor showed 68.5% homology to that of the human Inhibitor. We then constructed the expression plasmid pSV2a from pSV2-gpt and pc{alpha}1 and transfected It into COS-1 cells. The transfected cells synthe sized a molecule which was precipitated with anti-(rat {alpha}1 inhibitor)-IgG and had the same molecular size as that of the inhibitor produced by rat hepatocytes.

1This work was supported in part by a 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
E. Apletalina, J. Appel, N. S. Lamango, R. A. Houghten, and I. Lindberg
Identification of Inhibitors of Prohormone Convertases 1 and 2 Using a Peptide Combinatorial Library
J. Biol. Chem., October 9, 1998; 273(41): 26589 - 26595.
[Abstract] [Full Text] [PDF]

Home page
 JCBHome page
C. Pous, K. Chabin, A. Drechou, L. Barbot, T. Phung-Koskas, C. Settegrana, M.L. Bourguet-Kondracki, M. Maurice, D. Cassio, M. Guyot, et al.
Functional Specialization of Stable and Dynamic Microtubules in Protein Traffic in WIF-B Cells
J. Cell Biol., July 13, 1998; 142(1): 153 - 165.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y. Misumi, M. Sohda, A. Yano, T. Fujiwara, and Y. Ikehara
Molecular Characterization of GCP170, a 170-kDa Protein Associated with the Cytoplasmic Face of the Golgi Membrane
J. Biol. Chem., September 19, 1997; 272(38): 23851 - 23858.
[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.