| Identification of two discrete peptide: N-glycanases in Oryzias latipes during embryogenesis. | |
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MedLine Citation:
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PMID: 10460830 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Two different types of peptide:N-glycanase (PNGase) were identified in developing embryos of medaka fish ( Oryzias latipes ). Because the optimum pH values for their activities were acidic and neutral, they were designated as acid PNGase M and neutral PNGase M, respectively. The acid PNGase M corresponded to the enzyme that had been partially purified from medaka embryos (Seko,A., Kitajima,K., Inoue,Y. and Inoue,S. (1991) J. Biol. Chem., 266, 22110-22114). The apparent molecular weight of this enzyme was 150 K, and the optimal pH was 3.5-4.0, and the K m for L-hyosophorin was 44 microM. L-Hyosophorin is a cortical alveolus-derived glycononapeptide with a large N-linked glycan chain present in the perivitelline space of the developing embryo. Acid PNGase M was competitively inhibited by a free de-N-glycosylated nonapeptide derived from L-hyosophorin. This enzyme was expressed in ovaries and embryos at all developmental stages after gastrulation, but activity was not detected in embryos at developmental stages between fertilization and gastrula. Several independent lines of evidence suggested that acid PNGase M may be responsible for the unusual accumulation of free N-glycans derived from yolk glycoproteins (Iwasaki,M., Seko,A., Kitajima,K., Inoue,Y. and Inoue,S. (1992) J. Biol. Chem., 267, 24287-24296). In contrast, the neutral PNGase M was expressed in blastoderms from the 4-8 cell stage and in cells up to early gastrula. The general significance of these findings is that they show a developmental stage-dependent expression of the two PNGase activities, and that expression of the neutral PNGase M activity occurs concomitantly with the de-N-glycosylation of L-hyosophorin. These data thus support our conclusion that the neutral PNGase M is responsible for the developmental-stage-related de-N-glycosylation of the L-hyosophorin. |
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Authors:
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A Seko; K Kitajima; T Iwamatsu; Y Inoue; S Inoue |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Glycobiology Volume: 9 ISSN: 0959-6658 ISO Abbreviation: Glycobiology Publication Date: 1999 Sep |
Date Detail:
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Created Date: 1999-11-04 Completed Date: 1999-11-04 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 9104124 Medline TA: Glycobiology Country: ENGLAND |
Other Details:
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Languages: eng Pagination: 887-95 Citation Subset: IM |
Affiliation:
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Department of Biochemistry, Sasaki Institute, Kanda-Surugadai, Chiyoda-ku, Tokyo 101-0062, Japan. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amidohydrolases
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drug effects,
isolation & purification* Animals Blastoderm Female Fish Proteins Glycopeptides / metabolism Glycoproteins / metabolism* Hydrogen-Ion Concentration Isoenzymes / drug effects, isolation & purification Oryzias / embryology* Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase Substrate Specificity Sulfhydryl Reagents / pharmacology Tissue Distribution alpha-Fetoproteins / metabolism |
| Chemical | |
Reg. No./Substance:
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0/Fish Proteins; 0/Glycopeptides; 0/Glycoproteins; 0/Isoenzymes; 0/Sulfhydryl Reagents; 0/alpha-Fetoproteins; 123938-31-8/hyosophorin protein, Fish; EC 3.5.-/Amidohydrolases; EC 3.5.1.52/Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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