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

J. Biochem, 1974, Vol. 76, No. 4 721-733
© 1974 Japanese Biochemical Society

research-article

Snake Venom Proteinase Inhibitors

II. Chemical Structure of Inhibitor II Isolated from the Venom of Russell's viper (Vipera russelli)

Hidenobu TAKAHASHI, Sadaaki IWANAGA, Tsunehiro KITAGAWA*, Yasuji HOKAMA and Tomoji SUZUKI

Division of Plasma Proteins, Institute for Protein Research, Osaka University Suita, Osaka 565

The complete amino acid sequence of proteinase inhibitor II isolated from the venom of Russell's viper was established by Edman degradation and standard enzymatic and chemical techniques. The inhibitor consisted of 60 amino acid with histidine and lysine at the NH2– and COOH-termini, respectively. It has a molecular weight of 6,700 and was very basic. It contained 6 half-cystines in disulfide linkages; the locations of these half-cystine residues were determined by analyzing thermolytic fragments obtained from the native inhibitor II.

The overall primary structure of Russell's viper venom proteinase inhibitor II was very similar to that of bovine pancreatic basic trypsin inhibitor (Kunitz type) and cow colostrum trypsin inhibitor, having about 50 percent sequence homology. The 6 half-cystines of these three inhibitors were in the same positions in the amino acid sequences of the polypeptides. Moreover, the structural portions, which are found in the interior and the reactive site and tend to stabilize the unique structure of the Kunitz-type inhibitor, were found with extremely high sequence homology in proteinase inhibitor II. The evolution of these proteins is intriguing, since the evolutionary histories of cows and snakes are quite different.

*Present address: Faculty of Pharmaceutical Sciences, Nagasaki University, Nagasaki.


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
 Cold Spring Harb Symp Quant BiolHome page
T.E. Creighton and I.G. Charles
Biosynthesis, Processing, and Evolution of Bovine Pancreatic Trypsin Inhibitor
Cold Spring Harb Symp Quant Biol, January 1, 1987; 52(0): 511 - 519.
[Abstract] [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.