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 Kinoshita, K.
Right arrow Articles by Oikawa, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kinoshita, K.
Right arrow Articles by Oikawa, K.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 1988, Vol. 104, No. 5 827-831
© 1988 Japanese Biochemical Society

research-article

Purification and Characterization of ß-N-Acetylhexosaminidase I from Human Placenta1

Kenji Kinoshita*,2, Naoyuki Taniguchi*,3, Akira Makita*,4, Masaki Narita*,2 and Kiyoshi Oikawa**

*Biochemistry Laboratory, Cancer Institute, Hokkaido University School of Medicine Kita-ku, Sapporo, Hokkaido 060
**Department of Pediatric Dentistry, Hokkaido University School of Dentistry Kita-ku, Sapporo, Hokkaido 060

4 To whom all correspondence should be addressed

ß-N-Acetylhexosaminidase (hexosaminidase) I, which has an intermediate charge charac ter between those of hexosaminidases A({alpha}ß2 and B((ßß)2) was purified 1,500-fold from human placenta by procedures including chromatographies on concanavalin A (Con A)-Sepharose and an immunoadsorbent column. The isolated hexosaminidase I was heat-stable, and antigenically cross-reactive to anti-ß chain-IgG but not to anti- {alpha} chain IgG. The results of substrate specificity experiments using 3-labeled natural substrates indicated that the hexosaminidase I hydrolyzed Gb4Cer to Gb3 Cer but not GM2 to GM3 The tryptic peptide map of the hexosaminidase I was similar to that of hexosaminidase B, though some differences were observed. The hexosaminidase I after treatment with neuraminidase or endo-ß-N-acetylglucosaminidase H was partly converted to less acidic forms. Treatment of the hexosaminidase I with acid phosphatase did not change the charge character. Therefore hexosaminidase I is an acidic variant form of hexosaminidase B, possibly resulting from sialylation and the presence of phosphodiester bonds at the carbohydrate moiety.

1 This work was supported by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan and a grant from the Naito Science Foundation

2 Present addresses: Department of Pediatric Dentistry, Hokkaido University School of Dentistry, Kita-ku, Sapporo, Hokkaido 060

3 Department of Biochemistry, Osaka University Medical School, Kita-ku, Osaka, Osaka 530


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
 Clin. Chem.Home page
Y. Numata, A. Morita, Y. Kosugi, K. Shibata, N. Takeuchi, and K. Uchida
New sandwich ELISA for human urinary N-acetyl-{beta}-D-glucosaminidase isoenzyme B as a useful clinical test
Clin. Chem., April 1, 1997; 43(4): 569 - 574.
[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.