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Studies on biochemical properties of fish skin-mucus glycoproteins

Research Project

Project/Area Number 15580181
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Fisheries chemistry
Research InstitutionSaga University

Principal Investigator

HAMA Yoichiro  Saga University, Faculty of Agriculture, Associate Professor, 農学部, 助教授 (00243999)

Project Period (FY) 2003 – 2004
Project Status Completed (Fiscal Year 2004)
Budget Amount *help
¥2,600,000 (Direct Cost: ¥2,600,000)
Fiscal Year 2004: ¥900,000 (Direct Cost: ¥900,000)
Fiscal Year 2003: ¥1,700,000 (Direct Cost: ¥1,700,000)
Keywordsfish / skin mucus / glycoprotein / mucin / N-linked / O-linked / 粘質物
Research Abstract

This research was conducted to clarify the characteristics of fish skin-mucus glycoproteins. Five kinds of fish species that are indigenous to Ariake Sea, Mutsugoro, Warasubo, Hazekuchi, Akashitabirame, and Shoukihaze, were used for fish samples.
Fish skin-mucus was prepared from live fish samples. Glycoproteins in the skin-mucus were separated by Nuclease digestion, heat treatment, acid treatment, ion-exchange chromatography, and gel chromatography. Chromatographic behaviors on both ion-exchange and gel chromatographies of glycoproteins from Akashitabirame and Shoukihaze (the group I) was almost identical to those of glycoproteins from other fish species we had already studied so far. However, glycoproteins from Mutsugoro, Warasubo, and Hazekuchi (the group II) did not behaved similarly in both chromatographies.
Sugar compositional analysis of these glycoproteins revealed that : (1)total sugar contents of glycoproteins from the groups I and II were 50-75% and around 10%, respectively : (2)NeuAc and GalNAc were found dominantly in the group I, and GlcNAc,Gal,Man,NeuAc were found in the group II. Mannose is characteristic for N-linked glycoproteins but not for O-linked glycoproteins. Mannose had not been detected in glycoproteins isolated from fish mucus.
Sugar chains of the glycoproteins could be released by β-elimination and hydrazinolysis for the groups I and II, respectively. Therefore, glycoproteins from the groups I and II were confirmed to be O-linked and N-linked glycoproteins, respectively. Structure of major sugar chain from the group I was identical, and was identified to be NeuAcα2-6GalNAc. On other hand, structure of the major sugar chain from Mutsugoro (the group II) was presumed to be the complex type, which was composed of NeuAc,Gal,Man,and GlcNAc.

Report

(3 results)
  • 2004 Annual Research Report   Final Research Report Summary
  • 2003 Annual Research Report

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Published: 2003-04-01   Modified: 2016-04-21  

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