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

J. Biochem, 1988, Vol. 104, No. 4 667-670
© 1988 Japanese Biochemical Society

research-article

A Comparison of the Modes of Actions of Human Salivary and Pancreatic {alpha}-Amylases on Modified Maltooligosaccharides

Yuko Nagamine, Kaoru Omichi1 and Tokuji Ikenaka

Department of Chemistry, Osaka University College of Science Toyonaka, Osaka 560

1To whom correspondence should be addressed

The actions of three isozymes of human pancreatic {alpha}-amylase (HPA) on phenyl {alpha}-maltopentaoside, phenyl {alpha}-maltotetraoside, and their derivatives which have an iodo, an amino, or a carboxyl group at their first or penultimate glucopyranosyl residue from the non-reducing-end were examined. The results revealed that there was no difference in the actions of the three isozymes on the modified substrates and suggested the presence of five subsites (S3 S2, S1, S1', and S2' and a hydrophobic amino acid residue at subsite S33 in the active site of HPA. As compared with the action of human salivary {alpha}-amylase (HSA) on the same substrates, HPA had a tendency to release more phenyl {alpha}-glucoside from every substrate; however, an iodo, an amino, and a carboxyl group of the substrates had the same effects on the binding modes of the substrates to the active site of HPA as seen in the case of the salivary enzyme. This result indicates that the three-dimensional structures of the active sites of both {alpha}-amylases are quite similar except for some minor changes at subsites S3 and S2'


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




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.