TY - JOUR
T1 - Biochemical and thermodynamic characteristics of myoglobin from the skeletal muscle of sei whale Balaenoptera borealis
AU - Ochiai, Yoshihiro
AU - Watanabe, Yoshiaki
AU - Uchida, Naoyuki
AU - Ozawa, Hideo
AU - Watabe, Shugo
N1 - Copyright:
Copyright 2012 Elsevier B.V., All rights reserved.
PY - 2010
Y1 - 2010
N2 - Myoglobin (Mb) was purified from the skeletal muscle of a sei whale Balaenoptera borealis through a combination of ammonium sulfate fractionation and a series of column chromatography. The absorption maxima of the oxidized form appeared at 543 and 581 nm, while that of the met form appeared at 638 nm. The autooxidation rate at 25°C and pH 7.0 was calculated to be 0.04 h -1. The thermostability of this Mb at pH 7.0 as observed in the temperature dependency of circular dichroism (CD) showed that the apparent free energy of folding is -12.6 kJ/mol and the apparent melting temperature is 64.1°C. The a-helical content at 5°C and 80°C was 75.4% and 30.9%, respectively. Differential scanning microcalorimetry (DSC) showed that a large structural change took place at 81.8°C. CD measurement and DSC analysis gave considerable differences in the thermal denaturation profiles of this Mb, suggesting that the helices and hydrophobic interaction collapse in different temperature ranges. Finally, structural characteristics of this Mb were discussed based on the modeled tertiary structure.
AB - Myoglobin (Mb) was purified from the skeletal muscle of a sei whale Balaenoptera borealis through a combination of ammonium sulfate fractionation and a series of column chromatography. The absorption maxima of the oxidized form appeared at 543 and 581 nm, while that of the met form appeared at 638 nm. The autooxidation rate at 25°C and pH 7.0 was calculated to be 0.04 h -1. The thermostability of this Mb at pH 7.0 as observed in the temperature dependency of circular dichroism (CD) showed that the apparent free energy of folding is -12.6 kJ/mol and the apparent melting temperature is 64.1°C. The a-helical content at 5°C and 80°C was 75.4% and 30.9%, respectively. Differential scanning microcalorimetry (DSC) showed that a large structural change took place at 81.8°C. CD measurement and DSC analysis gave considerable differences in the thermal denaturation profiles of this Mb, suggesting that the helices and hydrophobic interaction collapse in different temperature ranges. Finally, structural characteristics of this Mb were discussed based on the modeled tertiary structure.
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U2 - 10.2331/suisan.76.686
DO - 10.2331/suisan.76.686
M3 - Article
AN - SCOPUS:77956055176
VL - 76
SP - 686
EP - 694
JO - Nippon Suisan Gakkaishi
JF - Nippon Suisan Gakkaishi
SN - 0021-5392
IS - 4
ER -