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Titolo:
Structure-function relationships of the two surface loops of myosin heavy chain isoforms from thermally acclimated carp
Autore:
Hirayama, Y; Sutoh, K; Watabe, S;
Indirizzi:
Univ Tokyo, Grad Sch Agr & Life Sci, Lab Aquat Mol Biol & Biotechnol, Bunkyo Ku, Tokyo 1138657, Japan Univ Tokyo Tokyo Japan 1138657 otechnol, Bunkyo Ku, Tokyo 1138657, Japan Univ Tokyo, Grad Sch Arts & Sci, Dept Life Sci, Meguro Ku, Tokyo 1538902, Japan Univ Tokyo Tokyo Japan 1538902 Life Sci, Meguro Ku, Tokyo 1538902, Japan
Titolo Testata:
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
fascicolo: 1, volume: 269, anno: 2000,
pagine: 237 - 241
SICI:
0006-291X(20000305)269:1<237:SROTTS>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
FAST SKELETAL-MUSCLE; TEMPERATURE-ACCLIMATION; SUBFRAGMENT-1 ISOFORMS; MOTOR FUNCTION; ACTIN; DICTYOSTELIUM; COMPLEX; DOMAIN; SUBSTITUTIONS; CONTRACTION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Sutoh, K Univ Tokyo, Grad Sch Agr & Life Sci, Lab Aquat Mol Biol & Biotechnol, Bunkyo Ku, Tokyo 1138657, Japan Univ Tokyo Tokyo Japan 1138657 Bunkyo Ku, Tokyo 1138657, Japan
Citazione:
Y. Hirayama et al., "Structure-function relationships of the two surface loops of myosin heavy chain isoforms from thermally acclimated carp", BIOC BIOP R, 269(1), 2000, pp. 237-241

Abstract

The structure-function relationships of fast skeletal myosin isoforms remain poorly understood. To shed some light, we constructed chimeric myosins comprised of Dictyostelium myosin heavy chain backbone with carp loop sequences and analyzed their functional properties. A loop 2-10 chimeric myosin having the loop 2 sequence of the fast skeletal isoform predominantly expressed in carp acclimated to 10 degrees C showed V-max in actin-activated Mg2+-ATPase activity 1.4-fold higher than a loop 2-30 chimera constructed from the loop 2 sequence of the dominant isoform in carp acclimated to 30 degrees C. These two chimera exhibited no significant differences in sliding velocity of actin filaments in in vitro motility assay. Contrastingly, both loop 1-associated chimeras, loop 1-10 and loop 1-30, did not differ in both ATPase activity and in sliding velocity of actin filaments. (C) 2000 AcademicPress.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/07/20 alle ore 20:51:32