Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
BIVALVE TROPOMYOSINS EXHIBIT STRONG INHIBITION OF ACTOMYOSIN MG-ATPASE AND HIGH-VISCOSITY
Autore:
NISHIMURA Y; OJIMA T; NISHITA K;
Indirizzi:
HOKKAIDO UNIV,FAC FISHERIES,DEPT CHEM HAKODATE HOKKAIDO 041 JAPAN HOKKAIDO UNIV,FAC FISHERIES,DEPT CHEM HAKODATE HOKKAIDO 041 JAPAN
Titolo Testata:
Fisheries science
fascicolo: 5, volume: 63, anno: 1997,
pagine: 802 - 806
SICI:
0919-9268(1997)63:5<802:BTESIO>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
MUSCLE ALPHA-TROPOMYOSIN; SKELETAL-MUSCLE; ADDUCTOR MUSCLES; AKAZARA SCALLOP; RABBIT; PROTEINS; HETEROGENEITY; TROPONINS; SEQUENCE;
Keywords:
BIVALVE; TROPOMYOSIN; INHIBITION OF MG-ATPASE; VISCOSITY;
Tipo documento:
Article
Natura:
Periodico
Citazioni:
33
Recensione:
Indirizzi per estratti:
Citazione:
Y. Nishimura et al., "BIVALVE TROPOMYOSINS EXHIBIT STRONG INHIBITION OF ACTOMYOSIN MG-ATPASE AND HIGH-VISCOSITY", Fisheries science, 63(5), 1997, pp. 802-806

Abstract

Tropomyosins were isolated from striated and smooth adductor muscles of akazara scallop Chlamys nipponensis akazara and ezo-giant scallop Patinopecten yessoensis and smooth adductor muscle of surf clam Spisulasacharinensis. These bivalve tropomyosins inhibited Mg-ATPase activity of rabbit reconstituted actomyosin to 15% of original activity, i.e., approximately 1.4 times stronger than rabbit and carp tropomyosins did at a weight ratio of 2:1 for F-actin: tropomyosin. On the other hand, the relative viscosities in the absence of KCl were 3.5-6 times higher than those of rabbit and carp tropomyosins. The intrinsic viscosities were, however, comparable to that of rabbit tropomyosin, i.e., 0.5dl/g for bivalve tropomyosins and 0.4 dl/g for rabbit tropomyosin. These viscosities suggest that the bivalve tropomyosins tend to form a highly polymerized form compared with rabbit tropomyosin. Circular dichroism spectra and amino acid compositions of the bivalve tropomyosins are similar to one another and also to rabbit and carp tropomyosins. C-terminal three amino acids of bivalve tropomyosins were sequenced as -Ala-Gly-Tyr (scallops) and -Gly-Tyr-Thr (surf clam), which are quite different from -Thr-Ser-Ile and Thr-Ser-Leu of rabbit alpha- and beta-tropomyosin, respectively.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 12/07/20 alle ore 06:37:52