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Titolo:
Induction of gelatinolytic activities in ayu muscle at the spawning stage
Autore:
Kubota, S; Kinoshita, M; Yokoyama, Y; Toyohara, H; Sakaguchi, M;
Indirizzi:
Kyoto Univ, Grad Sch Agr, Div Appl Biosci, Sakyo Ku, Kyoto 6068502, Japan Kyoto Univ Kyoto Japan 6068502 pl Biosci, Sakyo Ku, Kyoto 6068502, Japan Kochi Univ, Fac Agr, Lab Aquat Prod Utilizat, Nanko Ku, Kochi 7838502, Japan Kochi Univ Kochi Japan 7838502 Utilizat, Nanko Ku, Kochi 7838502, Japan Mukogawa Womens Univ, Interdisciplinary Res Inst Biosci, Nishinomiya, Hyogo 6638558, Japan Mukogawa Womens Univ Nishinomiya Hyogo Japan 6638558 Hyogo 6638558, Japan
Titolo Testata:
FISHERIES SCIENCE
fascicolo: 3, volume: 66, anno: 2000,
pagine: 574 - 578
SICI:
0919-9268(200006)66:3<574:IOGAIA>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
CONNECTIVE-TISSUE; MATURATION;
Keywords:
ayu; collagen; gelatinolytic activity; metalloproteinase; muscle; Plecoglossus altivelis; serine proteinase; spawning stage;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Citazioni:
9
Recensione:
Indirizzi per estratti:
Indirizzo: Toyohara, H Kyoto Univ, Grad Sch Agr, Div Appl Biosci, Sakyo Ku, Kyoto 6068502, Japan Kyoto Univ Kyoto Japan 6068502 akyo Ku, Kyoto 6068502, Japan
Citazione:
S. Kubota et al., "Induction of gelatinolytic activities in ayu muscle at the spawning stage", FISHERIES S, 66(3), 2000, pp. 574-578

Abstract

Gelatinolytic activities derived from both serine proteinase and metalloproteinase were induced in mature ayu muscle. These activities from ayu muscle at spawning stage (November) were fractionated successively by DEAE-cellulose, CM-cellulose, and gelatin affinity chromatographies, while no corresponding activity was detected from that of the growing stage (July). A gelatinolytic active band adsorbed to a CM-cellulose column was detected at 80 kDa by gelatin zymographic analysis. The activity was expressed at a slightly alkaline pH range and optimally at pH 8.5. The activity was inhibited by leupeptin and 1,10-phenanthroline, but not by E-64, suggesting that it was composed of both serine proteinase and metalloproteinase. Serine-type activity at 80 kDa was not adsorbed to a gelatin-immobilized column. On the other hand, metallo-type activity was adsorbed to the column, and the molecularmass of the activity was estimated to be 68 kDa. Our findings suggested that these gelatinolytic activities due to both serine proteinase and metalloproteinase, which are specifically induced in the spawning stage, are possibly responsible for collagen breakdown according to maturation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/10/20 alle ore 05:31:49