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STUDIES ON FUCOSYLTRANSFERASES RELATED TO BIOSYNTHESIS OF HUMAN BLOOD GROUP SUBST ANCES
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- YAZAWA SHIN
- Department of Legal Medicine, School of Medicine, Gunma University
Bibliographic Information
- Other Title
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- ヒトの血液型物質合成フコシルトランス フェラーゼに関する研究
- ヒト ノ ケツエキガタ ブッシツ ゴウセイ フコシル トランスフェラーゼ ニカ
- I. FUCOSYLTRANSFERASES IN HUMAN SALIVA
- I. ヒト唾液のフコシルトランス フェラーゼについて
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Description
Focosyltransferases catalize the transfer of 14C-fucose from GDP-L-fucose-14C to oligosaccharides from human milk were demonstrated in human saliva.<BR>1) An α- (1→4) -fucosyltransferase that synthesizes lacto-N-fucopentaose II and lacto-N-difucohexaose I from lacto-N-tetraose and lacto-N-fucopentaose I, respectively, was detected in saliva samples of Le (a-b+) secretors and Le (a+b-) non-secretors in which Lea substance was secreted.<BR>This enzyme activity was not detectable in saliva samples of Le (a-b-) secretors and nonsecretors, in which Lea substance was absent.<BR>2) An α- (1→2) -fucosyltransferase that synthesizes lacto-N-fucopentaose I from lacto-N-tetraose, was detected in saliva samples from Le (a-b+) secretors, secreted H and Leb substances, and from Le (a-b-) secretors, secreted only H substance.<BR>3) An α- (1→3) -fucosyltransferase was detected in all saliva samples from donors of different ABO and Lewis blood groups irrespective of their ABH secretor status.<BR>4) The fucosyltransferases were activated by Mn++ or Mg++ ions, and was inhibited completely with ATP, GTP and EDTA. They had a broad pH optimum between 5.0 and 7.0.<BR>5) Lacto-N-difucohexaose I could be synthesized from lacto-N-fucopentaose I by theα- (1→4) -fucosyltransferase from a saliva of OLe (a-b+) sec.donor.The difucohexaose could not be synthesized from lacto-N-fucopentaose II by the α- (1→2) -fucosyltransferase. Concerning the substrate specificities of the enzymes, it was, therefore, confirmed that H antigens could be converted to Leb antigens.
Journal
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- The KITAKANTO Medical Journal
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The KITAKANTO Medical Journal 26 (3), 203-215, 1976
The Kitakanto Medical Society
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Details 詳細情報について
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- CRID
- 1390001205333586688
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- NII Article ID
- 130003689687
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- NII Book ID
- AN0005179X
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- ISSN
- 13432826
- 18836135
- 00231908
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- NDL BIB ID
- 1710294
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- Data Source
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- JaLC
- NDL Search
- Crossref
- CiNii Articles
- OpenAIRE
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- Abstract License Flag
- Disallowed