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 Kwon, S.-T.
Right arrow Articles by Ohta, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kwon, S.-T.
Right arrow Articles by Ohta, T.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 1988, Vol. 104, No. 4 557-559
© 1988 Japanese Biochemical Society

research-article

Determination of the Positions of the Disulfide Bonds in Aqualysin I (a Thermophilic Alkaline Serine Protease) of Thermus aquaticus YT-1

Suk-Tae Kwon, Hiroshi Matsuzawa1 and Takahisa Ohta

Department of Agricultural Chemistry, The University of Tokyo Bunkyo-ku, Tokyo 113

2To whom correspondence should be addressed

Aqualysin I is a heat-stable alkaline serine protease produced by Thermus aquaticus YT-1. Aqualysin I comprises 281 amino acid residues and contains four cysteine residues. The cysteine residues seemed to form disulfide bonds in the molecule. Thus, the positions of the disulfide bonds were investigated. Disulfide bond-containing peptides were identified by peptide mapping with HPLC before and after carboxymethylation of chymotryptic peptides of aqualysin I. The disulfide bond-containing peptides were isolated and then carboxymethylated. Carboxymethylcysteine-containing peptides were purified, and their amino acid compositions and sequences were determined. Based on the data obtained and the primary structure of aqualysin I, it was concluded that two disulfide bonds were formed between Cys67 and Cys99, and between Cys163 and Cys194.


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 BiochemHome page
M. Sakaguchi, M. Takezawa, R. Nakazawa, K. Nozawa, T. Kusakawa, T. Nagasawa, Y. Sugahara, and M. Kawakita
Role of Disulphide Bonds in a Thermophilic Serine Protease Aqualysin I from Thermus aquaticus YT-1
J. Biochem., May 1, 2008; 143(5): 625 - 632.
[Abstract] [Full Text] [PDF]

Home page
 J BiochemHome page
M. Sakaguchi, M. Matsuzaki, K. Niimiya, J. Seino, Y. Sugahara, and M. Kawakita
Role of Proline Residues in Conferring Thermostability on Aqualysin I
J. Biochem., February 1, 2007; 141(2): 213 - 220.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. Withers-Martinez, J. W. Saldanha, B. Ely, F. Hackett, T. O'Connor, and M. J. Blackman
Expression of Recombinant Plasmodium falciparum Subtilisin-like Protease-1 in Insect Cells. CHARACTERIZATION, COMPARISON WITH THE PARASITE PROTEASE, AND HOMOLOGY MODELING
J. Biol. Chem., August 9, 2002; 277(33): 29698 - 29709.
[Abstract] [Full Text] [PDF]

Home page
 Microbiol. Mol. Biol. Rev.Home page
M. B. Rao, A. M. Tanksale, M. S. Ghatge, and V. V. Deshpande
Molecular and Biotechnological Aspects of Microbial Proteases
Microbiol. Mol. Biol. Rev., September 1, 1998; 62(3): 597 - 635.
[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.