TY - JOUR
T1 - Effect of high pressure treatment on cytoplasmic 5′-nucleotidase from rabbit skeletal muscle
AU - Mori, Sunao
AU - Yokoyama, Atsuko
AU - Iguchi, Reiko
AU - Yamamoto, Shuhei
AU - Suzuki, Atsushi
AU - Mizunoya, Wataru
AU - Tatsumi, Ryuichi
AU - Yoshioka, Keiko
AU - Ikeuchi, Yoshihide
N1 - Copyright:
Copyright 2011 Elsevier B.V., All rights reserved.
PY - 2007/6
Y1 - 2007/6
N2 - We investigated the effect of high-pressure treatment on the properties of cytoplasmic 5′-nucleotidase (NT), which converts inosine monophosphate (IMP) into inosine. After pressure treatment at 400 MPa, the activity of purified IMP-NT remained at almost 100%, but the activity of partially purified adenosine monophosphate (AMP)-NT decreased to about 40%. These data suggest that there is a difference in the pressure stability between the enzymes. In situ fluorescence spectroscopy of IMP-NT under pressure showed that its pressure-induced denaturation was reversible. When the pressure was reduced from the highest pressure to ambient pressure, hysteresis was observed. This suggests that high pressure treatment may lead to a partial change in the affinity of the subunits for each other once they have dissociated. The activities of IMP-NT and AMP-NT extracted from pressure-treated muscles decreased remarkably between 250 and 450 MPa, but IMP-NT was more stable than AMP-NT.
AB - We investigated the effect of high-pressure treatment on the properties of cytoplasmic 5′-nucleotidase (NT), which converts inosine monophosphate (IMP) into inosine. After pressure treatment at 400 MPa, the activity of purified IMP-NT remained at almost 100%, but the activity of partially purified adenosine monophosphate (AMP)-NT decreased to about 40%. These data suggest that there is a difference in the pressure stability between the enzymes. In situ fluorescence spectroscopy of IMP-NT under pressure showed that its pressure-induced denaturation was reversible. When the pressure was reduced from the highest pressure to ambient pressure, hysteresis was observed. This suggests that high pressure treatment may lead to a partial change in the affinity of the subunits for each other once they have dissociated. The activities of IMP-NT and AMP-NT extracted from pressure-treated muscles decreased remarkably between 250 and 450 MPa, but IMP-NT was more stable than AMP-NT.
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U2 - 10.1111/j.1745-4514.2007.00117.x
DO - 10.1111/j.1745-4514.2007.00117.x
M3 - Article
AN - SCOPUS:34249983453
SN - 0145-8884
VL - 31
SP - 314
EP - 327
JO - Journal of Food Biochemistry
JF - Journal of Food Biochemistry
IS - 3
ER -