JBC INTERFERin siRNA transfection reagent

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

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 Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Itoh, N.
Right arrow Articles by Yamashina, I.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Itoh, N.
Right arrow Articles by Yamashina, I.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J. Biol. Chem., Vol. 262, Issue 7, 3132-3135, Mar, 1987

Molecular cloning and sequence analysis of cDNA for batroxobin, a thrombin-like snake venom enzyme

N Itoh, N Tanaka, S Mihashi and I Yamashina

Determination of the nucleotide sequence of a cDNA for batroxobin, a thrombin-like enzyme from Bothrops atrox, moojeni venom, allowed elucidation of the complete amino acid sequence of batroxobin for the first time for a thrombin-like snake venom enzyme. The molecular weight of batroxobin is 25,503 (231 amino acids). The amino acid sequence of batroxobin exhibits significant homology with those of mammalian serine proteases (trypsin, pancreatic kallikrein, and thrombin), indicating that batroxobin is a member of the serine protease family. Based on this homology and enzymatic and chemical studies, the catalytic residues and disulfide bridges of batroxobin were deduced to be as follows: catalytic residues, His41, Asp86, and Ser178; and disulfide bridges, Cys7-Cys139, Cys26-Cys42, Cys74-Cys230, Cys118-Cys184, Cys150- Cys163, and Cys174-Cys199. The amino-terminal amino acid residue of batroxobin, valine, is preceded by 24 amino acids. This may indicate that the amino-terminal hydrophobic peptide (18 amino acids) is a prepeptide and that the hydrophilic peptide (6 amino acids), preceded by the putative prepeptide, is a propeptide.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
Z. Zhu, Z. Liang, T. Zhang, Z. Zhu, W. Xu, M. Teng, and L. Niu
Crystal Structures and Amidolytic Activities of Two Glycosylated Snake Venom Serine Proteinases
J. Biol. Chem., March 18, 2005; 280(11): 10524 - 10529.
[Abstract] [Full Text] [PDF]

Home page
 J BiochemHome page
Y. Kusano, Y. Yoshitomi, S. Munesue, M. Okayama, and K. Oguri
Cooperation of Syndecan-2 and Syndecan-4 among Cell Surface Heparan Sulfate Proteoglycans in the Actin Cytoskeletal Organization of Lewis Lung Carcinoma Cells
J. Biochem., January 1, 2004; 135(1): 129 - 137.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y. Zhang, A. Wisner, R. C. Maroun, V. Choumet, Y. Xiong, and C. Bon
Trimeresurus stejnegeri Snake Venom Plasminogen Activator. SITE-DIRECTED MUTAGENESIS AND MOLECULAR MODELING
J. Biol. Chem., August 15, 1997; 272(33): 20531 - 20537.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y. Zhang, A. Wisner, Y. Xiong, and C. Bon
A Novel Plasminogen Activator from Snake Venom
J. Biol. Chem., April 28, 1995; 270(17): 10246 - 10255.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1987 by the American Society for Biochemistry and Molecular Biology.