| The sugar-chain heterogeneity of human gamma-glutamyl transferases from the reproductive system and kidney. | |
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MedLine Citation:
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PMID: 2574643 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The sugar-chain heterogeneity of gamma-glutamyl transferase (gamma-GTP, EC 2.3.2.2) from the human reproductive system (seminal plasma, prostate and testis) and kidney was investigated using the serial lectin affinity technique and their properties were compared. According to the results of serial lectin affinity chromatography, a possible sugar chains of enzymes from reproductive system were mainly of the hybrid type without fucose linkages to the innermost GlcNAc and/or the biantennary complex type sugar chains and a few were of the multiantennary complex-type with branched GlcNAc (beta 1-4) Man and bisecting complex type sugar chains. On the contrary, the major sugar chains of kidney gamma-GTP were of the multiantennary complex type and/or bisecting complex type sugar chains. Results of isoelectric focusing showed the gamma-GTP bound multiantennary complex type sugar chains to be the most acidic glycoprotein. Moreover, the biantennary type sugar chains were slightly more acidic than the high mannose and/or hybrid type sugar chains, varying with the degree of sialylation. |
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Authors:
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K Arai; K Yoshida; T Komoda; N Kobayashi; H Saitoh; Y Sakagishi |
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Publication Detail:
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Type: Comparative Study; Journal Article |
Journal Detail:
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Title: Clinica chimica acta; international journal of clinical chemistry Volume: 184 ISSN: 0009-8981 ISO Abbreviation: Clin. Chim. Acta Publication Date: 1989 Sep |
Date Detail:
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Created Date: 1990-02-06 Completed Date: 1990-02-06 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 1302422 Medline TA: Clin Chim Acta Country: NETHERLANDS |
Other Details:
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Languages: eng Pagination: 75-84 Citation Subset: IM |
Affiliation:
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Department of Biochemistry, Saitama Medical School, Japan. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Adult Aged Carbohydrates / analysis* Chromatography, Affinity Concanavalin A Humans Isoelectric Focusing Isoenzymes / analysis* Kidney / enzymology* Lectins Male Prostate / enzymology* Semen / enzymology* Testis / enzymology* gamma-Glutamyltransferase / analysis* |
| Chemical | |
Reg. No./Substance:
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0/Carbohydrates; 0/Isoenzymes; 0/Lectins; 11028-71-0/Concanavalin A; EC 2.3.2.2/gamma-Glutamyltransferase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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