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Effects of temperature acclimation on calcium ATPase of the carp sarcoplasmic reticulum



Effects of temperature acclimation on calcium ATPase of the carp sarcoplasmic reticulum



Journal of Experimental Zoology 265(1): 9-17



The sarcoplasmic reticulum (SR) was prepared from the ordinary white muscle of carp Cyprinus capio acclimated to either 10 or 30 degree C over 5 weeks, and its Ca-2+-ATPase and Ca-2+ uptake activities measured. The SR Ca-2+-ATPase activities of the 10 and 30 degree C-acclimated carp were 0.2 and 0.1 mu-mol Pi/min cntdot mg at a reaction temperature of 10 degree C, respectively, and 1.1 and 0.6 mu-mol Pi/min cntdot mg at 30 degree C, respectively. The corresponding Ca-2+ uptake activities in the presence of sodium oxalate were 1.1 and 0.4 mu-mol Ca/min cntdot mg at 10 degree C, and 2.1 and 1.5 mu-mol Ca/min cntdot mg at 30 degree C, respectively. The break point in the Arrhenius plot of Ca-2+-ATPase activity was 9.2 degree C for the 10 degree C-acclimated SR and 15.9 degree C for the 30 degree -acclimated SR. The activation energy of Ca-2+-ATPase for the 10 degree C-acclimated SR between 10 and 40 degree C was 75 kJ/mol and similar to that for the 30 degree C-acclimated SR between 16 and 40 degree C, 81 kJ/mol. The membrane fluidity of SR, which was determined with a fluorescence probe, Py(3)Py, was higher for the 10 degree C-than 30 degree C-acclimated carp at any reaction temperature from 0 to 30 degree C. The peptide map in SDS-gels of Ca-2+-ATPase and alpha-chymotrypsin gave different pattern in the 40-70 kDa region between the two acclimated groups: the peptide of about 63k Da was specific to the 10 degree C-acclimated SR, while the peptide of about 50 kDa to the 30 degree C-acclimated SR. Tryptic peptide mapping also resulted in different fragmentation patterns in SDS-gels for the two Ca-2+-ATPases. These results suggest that carp would modify the fluidity of SR membrane and the molecular structure of Ca-2+-ATPase to compensate for fluctuating ambient temperatures.

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