Three isoforms of mammalian hyaluronan synthases have distinct enzymatic properties.

Itano, N; Sawai, T; Yoshida, M; Lenas, P; Yamada, Y; Imagawa, M; Shinomura, T; Hamaguchi, M; Yoshida, Y; Ohnuki, Y; Miyauchi, S; Spicer, A P; McDonald, J A; Kimata, K

Itano, N; Sawai, T; Yoshida, M; Lenas, P; Yamada, Y; Imagawa, M; Shinomura, T; Hamaguchi, M; Yoshida, Y; Ohnuki, Y; Miyauchi, S; Spicer, A P; McDonald, J A; Kimata, K.

Affiliation

Itano N; Institute for Molecular Science of Medicine, Aichi Medical University, Yazako, Nagakute, Aichi 480-1195, Japan.

J Biol Chem ; 274(35): 25085-92, 1999 Aug 27.

Article in En | MEDLINE | ID: mdl-10455188

Subject(s)

Glucuronosyltransferase/chemistry; Glycosyltransferases; Membrane Proteins; Transferases; Xenopus Proteins; Animals; Cell Line; Enzyme Stability; Gene Expression; Glucuronosyltransferase/genetics; Hyaluronan Synthases; Hyaluronic Acid/biosynthesis; Hyaluronic Acid/chemistry; Isoenzymes/chemistry; Kinetics; Microscopy, Phase-Contrast; Recombinant Proteins/chemistry; Substrate Specificity; Transfection; Uridine Diphosphate Glucuronic Acid/metabolism; Uridine Diphosphate N-Acetylglucosamine/metabolism

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Collection: 01-internacional Database: MEDLINE Main subject: Transferases / Glycosyltransferases / Glucuronosyltransferase / Xenopus Proteins / Membrane Proteins Limits: Animals Language: En Journal: J Biol Chem Year: 1999 Document type: Article

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