• Korean Journal of Food Science and Technology
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• v.18 no.3
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• pp.181-186
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• 1986

Myosin were prepared from red muscle and white muscle, and their ATPase activities were compared. Ca-ATPase activity of bovine myosin from red muscle was higher than that of myosin from white muscle, while Ca-ATPase activity of chicken myosin from red muscle differed hardly from that of myosin from whitemuscle. Atso EDTA-ATPase activity of bovine red muscle myosin was higher than that of white muscle myosin ,although EDTA-ATPase activity of chicken myosin from red muscle differed hardly from that of white muscle myosin. When myosins were treated with trypsin, bovine myosin from white muscle was hydrolysed moreeasily than red muscle myosin was. Chicken myosin from red muscle , however, was hydrolysed by trypsin more easily than white muscle myosin was.

• Journal of the East Asian Society of Dietary Life
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• v.16 no.4
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• pp.453-457
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• 2006

This study investigated the extractability, solubility, Mg$^{2+}$-, Ca$^{2+}$- and EDTA-ATPase activity of actomyosin prepared from leg and breast muscle of dog meat. The actomyosin extractability of breast muscle(2,100.6 mg/l00 g) was higher than that of leg muscle(500.8 mg/l00 g). The Mg$^{2+}$-ATPase activity of actomyosin had a high ionic strength of 0.02$\sim$0.05 M KCI and did not differ between leg and breast muscle. The Ca$^{2+}$-ATPase activity of actomyosin had a high ionic strength of 0.02$\sim$0.10 M KCI and leg muscle had a higher level of Ca$^{2+}$-ATPase activity than breast muscle did. The EDTA-ATPase activity was lower in low ionic strength and showed higher in high ionic strength, and increased sharply with increasing ionic strength up to 0.3 M KCI. The solubility of actomyosin did not differ between leg and breast muscle, and the solubility started and ended at KCI concentrations of 0.35 M and 0.4 M, respectively.

• Fisheries and Aquatic Sciences
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• v.8 no.1
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• pp.10-16
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• 2005

Conditions for sufficient and rapid distribution of a cryoprotectant (sorbitol solution) into intact fish muscle (Oncorhynchus mykiss) were studied as changing in the residual Ca2+ ATPase activity during freeze/thaw cycling. Chunks of the fish muscle were immersed in 4 concentrations of sorbitol solutions ($20\%$, $30\%$, $45\%$, and $60\%$) by a shaker mechanism at 5$^${circ}C. Whole immersion samples (W) showed a higher value of the residual Ca2+ ATPase activity than those in the untreated controls (C), except in the treated controls (TC), while less effect of immersion concentration could be found. Comparing the extent of penetration of sorbitol into the surface layer to inner layer of immersed fish chunks, outer portion samples achieved excellent cryoprotection with $100\%$ of the residual ATPase activity values or more. For the inner portion samples, $30\%$ and $45\%$ sorbitol solution treatments indicated a higher ATPase activity than $60\%$ treatment. At high concentrations, mass transfer rates during osmotic dehydration might berapid and it causes faster surface drying by dewatering at surface solute layer. Periodically immersed and relaxed samples, W (5-3-1), led to good cryoprotection effect: W (5-3-1) indicated high residual Ca2+ ATPase activity values and the residual ATPase activity values excess $100\%$ in immersion of $30\%$ and $45\%$ sorbitol solutions.

• Microbiology and Biotechnology Letters
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• v.8 no.2
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• pp.113-117
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• 1980

The effects of divalant metal ions on the ATPase activity were studied by using my of ibrillar protein of rabbit (Chin-Chilla species) fed with vegetable oils. The results obtained were as follows : 1. The ATPase activity in myofibrillar protein of the is not significant to Rabbit exhibited a common biohapsic respnse, such as the ATPase activity is high at a lower ionic strength and low at a higher ionic strength. 2. The effect of EDTA on the ATPase activity of Myofibrillar protein extracted from Rabbit fed vegetable oils was tested by using various concentrations. The ATPase activity was inhibited from 0.2mM and over concentration of EDTA. 3. The ATPase activity in Myofibrillar protein was decreased remarkably in 0.2mM and over concentration for $Mg^{2+}$, and in 1.0mM and over concentration for $Ca^{2+}$. 4. in vitro, the digestibilities in A, B, C and D groups of Rabbit muscle treated with Papsin and Trypsin for 30 minutes at 36$^{\circ}C$ water bath were 71.66％, 73.87％ ； 70.62％, 77.93％ ； 67.93％, 76.52％ ； and 86.79％, 90.22%, respectively.y.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.17 no.4
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• pp.271-279
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• 1984

Effects of temperature and additives on the stability of actomyosin extracted from skeletal muscle of Israeli carp, Cyprinus carpio nudus, were studied by analyzing free SH-group, ATP-sensitivity and Ca-ATPase activity. The used additives were sucrose, sorbitol, Na-glutamate and L-cysteine. Furthermore, the denaturation constant($K_D$), protective effect(${\Delta}E/M$) and the other thermo-dynamic parameters on protein denaturation are systematically discussed. The actomyosin showed $4.12{\sim}4.68 mg/ml$ in protein concentration, $2.63{\sim}2.93\%$ in ribonucleic acid to the protein, $1:2.20{\sim}2.63$ in the binding ratio of myosin and actin, $4.33{\sim}5.26\%$ in fat content, 109.78 in ATP-sonsitivity, $0.159{\sim}0.201\;{\mu}M-Pi/min/mg-protein$ in Ca-ATPase activity and $3.3{\sim}3.4M/10^5$g-protein in free SH-group content. The first-order rate plots were obtained on the decrease of Ca-ATPase activity and ATP-sensitivity with an increase in temperature, while the free SH-group was increased to $60^{\circ}C$ and decreased rapidly above the temperature. The half-life of Ca-ATPase activity on the actomyosin Ca-ATPase was 280 min at $12^{\circ}C$, 125 min at $20^{\circ}C$, 55 min at $30^{\circ}C$ and 13 min at $40^{\circ}C$, and activation energy, activation enthalpy, activation entropy and free energy of the proteins at $20^{\circ}C$ wene 5,395 cal/mole, 4,814 cal/mole, -40.42 e.u. and 17,626 cal/mole, respectively. The protective effect of the additives on the actomyosin Ca-ATPase showed that the most effective material is $3\%$ sorbitol and followed in the order of $8\%$ Na-glutamate, $1\%$ sucrose and $1\%$ L-cysteine. The actomyosin was more stable at $-30^{\circ}C$ than at $0^{\circ}C$ and $-20^{\circ}C$. and when the additives were used in the low temperature storage, $8\%$ Na-glutamate was the most effective. $3\%$ sorbitol, $1\%$ sucrose and $1\%$ L-cysteine was to become lower in the order.

• Proceedings of the Korean Biophysical Society Conference
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• 2001.06a
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• pp.66-66
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• 2001

Diabetic cardiomyopathy has been suggested to be caused by abnormal intracellular $Ca^{2＋}$ homeostasis in the myocardium, which is partly due to a defect in calcium transport by the cardiac sarcoplasmic reticulum (SR). In the present study, the underlying mechanism for this functional derangement was investigated with respect to SR $Ca^{2＋}$-ATPase and phospholamban (PLB, the inhibitor of SR $Ca^{2+}$-ATPase).(omitted)d)

• Journal of the Korean Society of Food Science and Nutrition
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• v.9 no.1
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• pp.45-50
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• 1980

Myofibrilar Protein from Korean Duck Muscle was extracted and ATPase activities were studied. The results were as follows: 1. Mg-activated ATPase activity of Myofibril from Korean Duck, muscle exhibited a biphasic response, ATPase activity was high at a low ionic strength and low activity was showed at high ionic strength. 2. Effect of EDTA on the Myofibrillar protein ATPase activity was studied, it was investigated that the EDTA inhibition was showed at the concentration of $6.9{\mu}g$ and it above. 3. It showed that the effect of Ca++ on ATPase activity was decreased at the lower than $3{\mu}g$. Inhibition showed at the concentration of $6.9{\mu}g$ and it above. 4. It showed that the effect of Mg++ on ATPase activity was decreased at the lower than $3.6{\mu}g$. Inhibition showed at the concentration of $3.9{\mu}g$ and it above.

• Journal of Plant Biology
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• v.33 no.4
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• pp.325-332
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• 1990

Light membrane vesicles were isolated from the zucchini hypocotyl by floatation on ficoll density gradients and the proteins were solubilized with Triton X100. Three ATP-hydrolyzing enzymes were partially purified by ion-exchange and gel filtration chromatography and isoelectric focusing. There are plasma membrane-type ATPase whose activity was inhibited by vanadate but not by nitrate, tonoplast-type ATPase which was sensitive to nitrate but insensitive to vanadate and one having a phosphatase activity with a pI value different from that of an acid phosphatase. A fraction was obtained after DEAE-ion-exchange chromatography crossreacting with polyclonal antibodies against Ca2+ -ATPase from human erythrocytes.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.25 no.2
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• pp.73-78
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• 1992

To investigate the desirable index for evaluation of frozen surimi's grades, the relationship between indices for grading of surimi, such as ATPase activity $(Ca^{2+}-,\;Mg^{2+}-\;and\;EDTA-)4, solubility, viscosity and K-value of frozen surimi and jelly strength of kamaboko was studied. The myofibrillar $Ca^{2+}-ATPase$ activity and solubility from frozen surimi of grades SA, FA, A, RA and B gave values of $1.184\pm0.2,\;0.956\pm0.14,\;0.766\pm/0.07,\;0.453\pm0.07\;and\;0.227\pm0.08$(umoles Pi/min/mg) for $Ca^{2+}-$ATPase activity and $93.19\pm5,\;84.62\pm4,\;70.63\pm5,\;41.21\pm4\;and\;32.82\pm4(\%)$ for solubility, respectively. Therefore, the myofibrillar $Ca^{2+}-$ATPase activity and solubility of surimi were closely related to the jelly strength of kamaboko from same material, as the correlation coefficient were 0.9584 and 0.9849, respectively. K-value, the index of freshness, was related to the jelly strength of frozen surimi as the correlation coefficient 0.9053 and shown as SA $15.67\pm1.4,\;FA\;14.94\pm 3,\;A\;28.00\pm5,\;RA\;32.16\pm3\;and \;B\;48.68\pm 5(\%)$. $Mg^{2+}-$ and EDTA-ATPase activity and viscosity were not related to the jelly strength. The $Ca^{2+}-$ATPase activity and solubility were found to be useful index for evaluating the quality of frozen surimi.

• Journal of Plant Biotechnology
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• v.36 no.1
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• pp.59-63
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• 2009

Calcium ion ($Ca^{2+}$) is thought to play the important role as a second messenger for signal transduction that results in various physiological responses to cope with developmental programs and environmental changes in plant. In plant cells, the central vacuole functions as a major calcium store, which is important for both signal transduction and preventing cytotoxicity. Although there is evidence for the biochemical characterizations of a calmodulin-regulated $Ca^{2+}$-ATPase (ACA11) localized to vacuole membrane, the biological function to ACA11 in plant has not been verified. In this study, we show that the cell death as the hypersensitive response (HR) in mature leaves is induced in transgenic plant of a vacuole ACA-type $Ca^{2+}$-ATPase, ACA11. Evidence that cell death phenotype is the result of ACA11 gene silencing is provided by Western blot assay using membrane fraction proteins extracted from transgenic plant. The 3, 3'-diaminobenzidine (DAB) staining study provides that the cell death is caused by the increase of reactive oxygen species (ROS) in mature leaves of transgenic plants.