1994 Fiscal Year Final Research Report Summary
Microstructure of Sialoglycoprotein Obtained From Hen' s Egg White And Its Biological Activities.
| Project/Area Number |
05806034
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
Zootechnical science/Grassland science
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| Research Institution | Gifu University |
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Principal Investigator |
WATANABE Kenji Gifu University, Faculty of Agriculture, Professor, 農学部, 教授 (70023447)
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| Co-Investigator(Kenkyū-buntansha) |
SHIMOYAMADA Makoto Gifu University, Faculty of Agriculture, Assistnat, 農学部, 助手 (60235695)
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| Project Period (FY) |
1993 – 1994
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| Keywords | Egg white Protein / Ovomucin / Antivirus Activity / Antitumor Activity |
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| Research Abstract |
In this study, sialoglycoproteins (ovomucin, ovomucoid, ovoflavoprotein and ovoglycoprotein) were prepared from hen' s egg white and their biological activities (antitumor activities against SR-180 and MH134 cell, and inhibitory activities of hemagglutination by rotavirus and newcastle disease virus) were determined. Ovomucin was found to have the specific higher activities among the used sialoglycoproteins. alpha-Ovomucin (particle weight about 180,000) and beta-ovomucin (particle weight about 400,000) were fractionated form sonicated ovomucin and their activities were also determined. beta-Ovomucin was found to show higher activities than alpha-ovomucin. From the pronase-digested ovomucin and beta-ovomucin, their fragments were separated by ion-exchange and gel-filtration column chromatographies. And the relationship between biological activities and chemical composition of each fragment was compared. It was demonstrated that beta-ovomucin was comprised of two carbohydrate-rich parts containing 0-linked carbohydrate chain (molecular weight about 120,000) and three carbohydrate-poor parts containing N-linked carbohydrate chain (moleular weight about 50,000) . And the former was mainly concerned in the biological activities. In generally, biological activities of ovomucin were demonstrated to present by the action of carbohydrate chain containing sialic acid linked with peptide chain, as seen in carbohydrate-rich parts in beta-ovomucin.
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