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Titolo:
THERMAL UNFOLDING OF THE COLD-ACCLIMATED TYPE OF CARP LIGHT-MEROMYOSIN EXPRESSED BY RECOMBINANT-DNA IN ESCHERICHIA-COLI
Autore:
KAKINUMA M; FUNABARA D; NAKAYA M; HIRAYAMA Y; WATABE S; MAEDA K; OOI T;
Indirizzi:
UNIV TOKYO,GRAD SCH AGR & LIFE SCI,LAB AQUAT MOL BIOL & BIOTECHNOL TOKYO 113 JAPAN UNIV TOKYO,GRAD SCH AGR & LIFE SCI,LAB AQUAT MOL BIOL & BIOTECHNOL TOKYO 113 JAPAN MATSUSHITA ELECT IND CO LTD,INT INST ADV RES KYOTO 61902 JAPAN KYOTO WOMENS UNIV,DEPT FOOD SCI KYOTO 605 JAPAN
Titolo Testata:
Fisheries science
fascicolo: 6, volume: 63, anno: 1997,
pagine: 1008 - 1013
SICI:
0919-9268(1997)63:6<1008:TUOTCT>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
DIFFERENTIAL SCANNING CALORIMETRY; FAST SKELETAL-MUSCLE; TEMPERATURE-ACCLIMATION; MYOSIN SUBFRAGMENT-1; ROD DOMAIN; PROTEINS; STABILITY; ISOFORMS; CONFORMATION; SITE;
Keywords:
LIGHT MEROMYOSIN; CARP; ALPHA-HELIX; DIFFERENTIAL SCANNING CALORIMETRY; CIRCULAR DICHROISM; BACTERIAL EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Citazioni:
30
Recensione:
Indirizzi per estratti:
Citazione:
M. Kakinuma et al., "THERMAL UNFOLDING OF THE COLD-ACCLIMATED TYPE OF CARP LIGHT-MEROMYOSIN EXPRESSED BY RECOMBINANT-DNA IN ESCHERICHIA-COLI", Fisheries science, 63(6), 1997, pp. 1008-1013

Abstract

cDNA encoding fast skeletal muscle light meromyosin (LMM) predominantly expressed in carp acclimated to a cold temperature of 10 degrees C was inserted into an Escherichia coli expression vector pET-11a. The resulting plasmid pET10 produced non-fused carp 10 degrees C-type LMM, yielding 10% of the total proteins in E. coli. The 10 degrees C-type LMM was purified by altered dialyses against high-and low-ionic-strength buffers and ion-exchange chromatography. An apparent molecular mass of the purified LMM was about 74,000 on SDS-PAGE, which was slightly larger than that previously reported for LMM isolated from carp acclimated to 10 degrees C. Transition temperatures (Tm) were 30.2 and 34.9 degrees C for the present 10 degrees C-type LMM on DSC analysis. This LMM exhibited a typical pattern of alpha-helix in CD spectroscopy with two minima at 222 and 208 nm, and its alpha-helical content at 20 degrees C was about 70%. The maximal decreasing rate derivative at 35 degrees C of the mean residue ellipticity of carp LMM per unit change of measuring temperature well reflected Tm values observed in DSC analysis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/06/20 alle ore 01:43:00