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Titolo:
Interaction of cytotoxic bicyclic peptides, theonellamides A and F, with glutamate dehydrogenase and 17 beta-hydroxysteroid dehydrogenase IV
Autore:
Wada, S; Matsunaga, S; Fusetani, N; Watabe, S;
Indirizzi:
Univ Tokyo, Dept Aquat Biosci, Grad Sch Agr & Life Sci, Bunkyo Ku, Tokyo 1138657, Japan Univ Tokyo Tokyo Japan 1138657 Life Sci, Bunkyo Ku, Tokyo 1138657, Japan
Titolo Testata:
MARINE BIOTECHNOLOGY
fascicolo: 3, volume: 2, anno: 2000,
pagine: 285 - 292
SICI:
1436-2228(200005/06)2:3<285:IOCBPT>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
MOLECULAR-CLONING; SPONGE; GLYCOPEPTIDE; SWINHOEI; GENE;
Keywords:
theonellamide; glutamate dehydrogenase; 17 beta-hydroxysteroid dehydrogenase IV; marine toxin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Citazioni:
17
Recensione:
Indirizzi per estratti:
Indirizzo: Watabe, S Univ Tokyo, Dept Aquat Biosci, Grad Sch Agr & Life Sci, Bunkyo Ku, Tokyo 1138657, Japan Univ Tokyo Tokyo Japan 1138657 Bunkyo Ku, Tokyo 1138657, Japan
Citazione:
S. Wada et al., "Interaction of cytotoxic bicyclic peptides, theonellamides A and F, with glutamate dehydrogenase and 17 beta-hydroxysteroid dehydrogenase IV", MAR BIOTEC, 2(3), 2000, pp. 285-292

Abstract

Theonellamide A, a bicyclic peptide isolated from a Theonella sponge, was fixed on hydrazide-containing gel beads and screened for its binding proteins from rabbit liver tissues. Analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed that two major proteins of 80 kDa and 55 kDa interacted with theonellamide A. The interaction between theonellamide A and two proteins was confirmed by competition experiments in which these two proteins failed to bind to theonellamide A-conjugated gel beads in the presence of theonellamide A or F. Amino-terminal amino acid sequence analysis of peptide fragments derived from the binding proteins by lysylendopeptidase digestion demonstrated that the 80-kDa and 55-kDa proteins were 17 beta-hydroxysteroid dehydrogenase IV and glutamate dehydrogenase, respectively. In an in vitro assay system, amination of alpha-ketoglutarate by glutamate dehydrogenase was activated with theonellamide F, although this effect was weaker than that with adenosine diphosphate, a well-known activator.

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Documento generato il 06/07/20 alle ore 05:39:15