Purification and characterization of metmyoglobin reductase from ordinary muscle of blue‐fin tuna View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2000-06

AUTHORS

Ching‐Yung Pong, Tze‐Kuei Chiou, Fang‐Pei Nieh, Shann‐Tzong Jiang

ABSTRACT

Metmyoglobin (Met-Mb) reductase from blue-fin tuna ordinary muscle was purified to electrophoretical homogeneity by ammonium sulfate fractionation, ion exchange and organomercurial agarose affinity chromatography. The molecular weight estimated by SDS-PAGE was 100 kDa. The optimal pH and temperature for the reduction of met-Mb were 7.3 and 25°C, respectively. This enzyme was very stable at pH 7.0–7.3 and 4°C–15°C. The purified enzyme was strongly activated by K+, moderately activated by Na+ and Mn2+, but not affected by Ni2+. It was moderately inhibited by Li+, NH4+, Mg2+, and Co2+. The Vmax for the reduction of met-Mb and NADH were 0.32 and 0.43 mM/min/mg, while Km were 2.3 × 10−5 and 24.4 × 10−5 M, respectively. More... »

PAGES

599-604

Journal

TITLE

Fisheries Science

ISSUE

3

VOLUME

66

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1046/j.1444-2906.2000.00093.x

DOI

http://dx.doi.org/10.1046/j.1444-2906.2000.00093.x

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1011463789


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