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Titolo:
Isolation and characterization of a novel 45 kDa calponin-like protein from anterior byssus retractor muscle of the mussel Mytilus galloprovincialis
Autore:
Funabara, D; Nakaya, M; Watabe, S;
Indirizzi:
Univ Tokyo, Lab Aquat Mol Biol & Biotechnol, Grad Sch Agr & Life Sci, Bunkyo Ku, Tokyo 1138657, Japan Univ Tokyo Tokyo Japan 1138657 Life Sci, Bunkyo Ku, Tokyo 1138657, Japan
Titolo Testata:
FISHERIES SCIENCE
fascicolo: 3, volume: 67, anno: 2001,
pagine: 511 - 517
SICI:
0919-9268(200106)67:3<511:IACOAN>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMINO-ACID-SEQUENCE; GIZZARD SMOOTH-MUSCLE; FORCE PRODUCTION; IN-VITRO; PHOSPHORYLATION; MYOSIN; CATCH; PARAMYOSIN; GENE; IDENTIFICATION;
Keywords:
actomyosin; anterior byssus retractor muscle; calponin; catch; Mg2+-ATPase; Mytilus galloprovincialis;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Watabe, S Univ Tokyo, Lab Aquat Mol Biol & Biotechnol, Grad Sch Agr & LifeSci, Bunkyo Ku, Tokyo 1138657, Japan Univ Tokyo Tokyo Japan 1138657 Bunkyo Ku, Tokyo 1138657, Japan
Citazione:
D. Funabara et al., "Isolation and characterization of a novel 45 kDa calponin-like protein from anterior byssus retractor muscle of the mussel Mytilus galloprovincialis", FISHERIES S, 67(3), 2001, pp. 511-517

Abstract

A calponin-like protein of 45 kDa was isolated from mussel anterior byssusretractor muscle (ABRM) and its inhibitory effects on actomyosin Mg2+-ATPase was demonstrated. The 2-D electrophoresis for ABRM myofibrils gave a spot of 45 kDa protein in addition to myofibrillar proteins such as myosin andactin. The 45 kDa protein, which was more basic and showed a slightly higher molecular weight than actin, was isolated by ion-exchange chromatographyand subjected to chymotryptic digestion. N-terminal amino acid sequencing of polypeptide fragments produced gave two sequences, ASQKGMTSFGAVRHH and GMDRALISKMGSKYDSGL, both of which showed a high homology to those of vertebrate calponins and invertebrate calponin-related proteins. Furthermore, the 45 kDa protein strongly reacted with commercially available antibody raisedagainst chicken smooth muscle calponin, demonstrating that the mussel ABRM45 kDa protein is a new member of the calponin family. Then, actomyosin Mg2+-ATPase activity of ABRM was measured in the presence and absence of the 45 kDa protein. The 45 kDa protein clearly inhibited actomyosin Mg2+-ATPaseactivity in a dose-dependent manner as in the case of other vertebrate calponins. These results indicate that the 45 kDa calponin-like protein is involved in the thin filament-associated regulation of molluscan smooth musclecontraction, possibly of a unique contraction called catch.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 10/07/20 alle ore 09:46:42