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

J. Biochem, 1982, Vol. 92, No. 3 709-716
© 1982 Japanese Biochemical Society

research-article

Human Lysozyme-Catalyzed Reaction of Chitooligosaccharides1

Tamo FUKAMIZO2,*, Takao TORIKATA**, Satoru KUHARA* and Katsuya HAYASHI*

*Department of Agricultural Chemistry, Faculty of Agriculture, Kyushu University Higashi-ku, Fukuoka, Fukuoka 812
**Faculty of Agriculture, Kyushu Tokai University Choyomura, Aso, Kumamoto 869–14

2 To whom correspondence should be addressed.

The time-courses of the human lysozyme-catalyzed reaction of chitopentaose were measured by high-performance gel-filtration in comparison with those of hen egg-white lysozyme. Human lysozyme has considerably larger rate constants for the cleavage of glycosidic linkages and transglycosylation than those of hen lysozyme, in agreement with the fact that human lysozyme exhibits a large lytic activity.

It has been reported that binding subsite D in human lysozyme has negative free energy on substrate binding, whereas subsite D in hen lysozyme has unfavorable positive free energy due to the distortion of a sugar residue. The time-courses calculated under the assumption that subsite D in human lysozyme has negative free energy on substrate binding did not fit the experimentally obtained time-courses, even though the combination of values of rate constants in the enzymatic reaction widely varied in the calculation of the time-courses. Thus, it was concluded that subsite D in human lysozyme may not have negative binding free energy, but positive values similar to hen lysozyme.

1 This study was partly supported by a Grant-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
 GlycobiologyHome page
T. Fukamizo, A. Fleury, N. Cote, M. Mitsutomi, and R. Brzezinski
Exo-{beta}-D-glucosaminidase from Amycolatopsis orientalis: catalytic residues, sugar recognition specificity, kinetics, and synergism
Glycobiology, November 1, 2006; 16(11): 1064 - 1072.
[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.