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Titolo:
THERMAL-DENATURATION OF BETA-CONNECTIN ISOLATED FROM CARP MUSCLE
Autore:
SEKI N; KUMANO Y;
Indirizzi:
HOKKAIDO UNIV,FAC FISHERIES,FOOD BIOCHEM LAB,MINATO KU HAKODATE HOKKAIDO 041 JAPAN
Titolo Testata:
Fisheries science
fascicolo: 2, volume: 61, anno: 1995,
pagine: 315 - 319
SICI:
0919-9268(1995)61:2<315:TOBIFC>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
FROG SKELETAL-MUSCLE; IMMUNOELECTRON MICROSCOPY; POSTMORTEM CHANGES; ALPHA-CONNECTIN; TITIN; FILAMENTS; PROTEIN; MYOSIN; ACTIN;
Keywords:
MUSCLE PROTEIN; CONNECTIN; TITIN; DENATURATION; CARP;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
23
Recensione:
Indirizzi per estratti:
Citazione:
N. Seki e Y. Kumano, "THERMAL-DENATURATION OF BETA-CONNECTIN ISOLATED FROM CARP MUSCLE", Fisheries science, 61(2), 1995, pp. 315-319

Abstract

beta-Connectin, a 2,100 kDa fragment of connectin, was extracted with0.1 M phosphate buffer at pH 6.6 and purified on a Bio-Gel A 50 m gelfiltration from carp skeletal myofibrils. The isolated connectin was in the native state judging from the fact that it enhanced aggregationof both myosin and actin filaments and appreciably elevated actomyosin Mg-ATPase activity. The thermal denaturation of connectin was measured in 0.1 M and 0.6 M KCl solutions of neutral pH by means of turbidity. Increase in turbidity was observed at 40 degrees C and occurred markedly above 50 degrees C. A physiological concentration of Ca2+ and Mg2+ did not affect turbidity. The loss of interaction of connectin withmyosin was caused by the denaturation of myosin at lower temperaturesrather than that of connectin.

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Documento generato il 07/07/20 alle ore 15:29:33