• Applied Biological Chemistry
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• v.41 no.2
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• pp.130-136
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• 1998

Microsomes of tomato roots were prepared and the activities of microsomal ATPases were measured in order to understand the molecular mechanisms of various ion transports. The activities of plasma membrane $H^+-ATPase$ and vacuolar $H^+-ATPase$ were evaluated to ${\sim}30%$ and ${\sim}38%$ of total microsomal ATPase activity by using their specific inhibitor, vanadate and nitrate $(NO^-_3)$, respectively. The inhibitory effects of vanadate and $NO^-_3$ were additive and the simultaneous additions of these two inhibitors decreased the total activity up to $50{\sim}70%$. The microsomal ATPase activity was regulated key pH and the maximal activity was obtained at pH 7.4. The activity of microsomal ATPase was increased by $K^+$ up to ${\sim}30%$ at the concentration of $K^+$ above 10 mM. However, the $K^+-induced$ increase in the activity was completely inhibited by the simultaneous addition of $Na^+$. To identify the ATPase activity regulated by $K^+$, the effects of specific inhibitors were measured. Vanadate and $NO^-_3$ inhibited total ATPase activity by 27% and 32% in the absence, of $K^+$ and by 27% and 40% in the presence of 120 mM $K^+$, respectively. These results suggest that $K^+$ increases the activity of $NO^-_3-sensitive$ vacuolar $H^+-ATPase$ but not that of vanadate-sensitive plasma membrane $H^+-ATPase$ since vanadate has no effect on $K^+-induced$ increase in ATPase activity. The microsomal ATPase activity was also decreased by increasing $Ca^{2+}$ concentration. Interestingly, $NO^-_3$ blocked the $Ca^{2+}-induced$ inhibition of microsomal ATPase activity; however, vanadate had no effect. These results imply that vacuolar $H^+-ATPase$ is activated by $K^+$ and inhibited by $Ca^{2+}$.

• Applied Microscopy
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• v.27 no.2
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• pp.111-120
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• 1997

Cylinder-like crystals of $Ca^{2+}-ATPase$ provide views parallel to the lamellar plane, from which parameters of lamellar stacking can be directly measured. These parameters were measured using different preparation methods. Assuming that molecular packing is the same, data from lamellar plane could supplement those obtained by tilting large, thin plate-like crystals. However, base on data obtained .by electron microscopy and x-ray powder patterns, the plate-like crystal may have another scheme for stacking the lamellar. The projection map (h, 0, 1) from cylinder-like crystals using cryoelectron microscopy suggest the lamellar spacing can be variable.

• The Korean Journal of Physiology
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• v.21 no.2
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• pp.157-167
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• 1987

Benzyl alcohol is known to have dual effect on the red blood cell shape change. At low concentration up to 50 mM benzyl alcohol transformed the shape from discocyte to stomatocyte by preferent binding to the inner hemileaflet, however, at higher concentratransformed the shape from discocyte to stomatocyte by preferential binding to the inner monolayer, however, at higher concentration above 50 mM benzyl alcohol transformed to echinocyte by affecting both monolayers. These results suggest that the effect of benzyl alcohol on the red blood cell shape and $Ca^{++}$ transport across cardiac cell membranes to assess the effects of the drug on the structures and functions of the biological cell membranes. The results are as follows: 1) Benzyl alcohol up to 40 mM caused progressive stomatocytic shap change of the red blood cell but above 50 mM benzyl alcohol caused echinocytic shape change. 2) Benzyl alcohol up to 40 mM inhibited both osmotic hemolysis and osmotic volume change of the red blood cell in hypotonic and hypertonic NaCl solutions, respectively. 3) Benzyl alcohol inhibited both Bowditch Staircase and Wood-worth Staircase phenomena at rat left auricle. 4) Benzyl alcohol at concentration of 5 mM increased $Ca^{++}-ATPase$ activity of red blood cell ghosts slightly but above S mM benzyl alcohol inhibited the $Ca^{++}-ATPase$ activity. 5) Benzyl alcohol at concentrations of 5 mM and 10 mM increased $Ca^{++}-ATPase$ activity slightly at rat gastrocnemius muscle S.R. but above 10 mM benzyl alcohol inhibited the $Ca^{++}-ATPase$ activity. Above results indicate that benzyl alcohol inhibit water permeability and $Ca^{++}$ transport across cell membranes in part via effects on the fluidity and transition temperatures of the bulk lipid by preferential intercalation into cytoplasmic monolayer and in part via other effect on the conformational change of active sites of the $Ca^{++}-ATPase$ molecule extended in cytoplasmic face.

• 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.

• The Korean Journal of Physiology
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• v.11 no.2
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• pp.1-7
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• 1977

The activity of the $Ca^{++}$ activated adenosinetriphosphatase (Ca-ATPase) of actomyosin systeme of rabbit and frog skeletal muscle has been studied at varying pH and temperature. The PH optima of the Ca-ATPase activity of the rabbit actomyosin was rather broad. Over the temperature range of $16-36^{\circ}C$ activity of the enzyme was not appreciably changed between pH 6.4-8.5; below and above which it rapidly reduced. The pH at the inflection point of the enzyme activity increased as temperature decreased, showing the ${\bigtriangleup}pH\;inflection/{\bigtriangleup}T$ of approximately $-0.018\;unit/^{\circ}C$. Consequently, $(OH^-)/(H^+)$ ratio at the inflection point was constant regardless of assay temperature. In the frog actomyosin systems the Ca-ATPase activity was not apparently altered between PH 6.4-7.0 when the incubation temperature was $15{\sim}30^{\circ}C$. Outside of this range of pH, however, the enzyme activity was dramatically decreased. The pH of the inflection point changed inversely with temperature. ${\bigtriangleup}pH\;inflection/{\bigtriangleup}T$ at the acidic side was approximately $-0.018\;unit/^{\circ}C$, whereas that at the alkaline side it was about $-0.037\;unit/^{\circ}C$. The Arrhenius Plot on the Ca-ATPase activity at constant $(OH^-)/(H^+)$ ratio of 1.0 was not linear, but showed break at arround $20^{\circ}C$ for both rabbit and frog actomyosin Preparations. From these results it was speculated that pH dependence of Ca-ATPase activity of rabbit actomyosin systems might reflect titrations of histidine-imidazole and -SH groups, and that of the frog actomyosin represents titrations of histidine-imidazole and lysyllysine ${\alpha}-NH_2$ groups.

• 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.

• The Korean Journal of Zoology
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• v.13 no.3
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• pp.85-93
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• 1970

Measurements were made of the $Ca^++$ uptake, oxygen consumption and ATPase activity of mitochondria extracted from the rat liver in sucrose-tris chloride medium. $Ca^++$ binding of mitochondria was not affected by the incubation temperature in the range of $0^\\circ - 37^\\circ C$. Succinate did not increase the amount of $Ca^++$ bound while it increased oxygen consumption highly. The presence of ATP in the incubation medium did not enhance the $Ca^++$ uptake either. Therefore, it is concluded that the initial binding of $Ca^++$ is independent on metabolism.

• The Korean Journal of Food And Nutrition
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• v.10 no.2
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• pp.151-159
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• 1997

In order to compare and examine the general characteristics of myofibrillar proteins which is an important protein source as a food resource and relates directly with muscle contraction, we have extracted the myofibrillar proteins from squid and clam. The ionic strength of myofibrillar proteins connected with Ca-ATPase activity, Mg-ATPase activity and EDTA-ATPase activity showed distinct differences between squid and clam. In the activity-pH curve, actomyosin of the clam had a weak biphasic response. In the low concentration of dioxane, myofibrillar proteins of the squid showed a sudden decrease in activity but myofibrillar proteins of the clam showed in increase in activity. Ethanol and metanol in low concentration caused myosin and HMM from the squid and clam to increase their activities. If we cause modification by NEM, under 10-6M concentration, the activity was increased but above 10-5M concentration, there was a sudden decrease in activity.

• The Korean Journal of Physiology
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• v.10 no.1
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• pp.1-5
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• 1976

The trypanocidal drug suramin, an impermeant polyanion, has been shown to be a powerful inhibitor of the calcium uptake and calcium-stimulated ATPase activity of sarcoplasmic reticulum (Fortes et al., 1974). In view of this finding, an attempt was made to investigate the effect of suramin on $Ca^{++}$ transport in resealed red cells and on $Ca^{++}$-activated ATPase in red blood cell membrane fragments (RBCMF). The results obtained are summarized as follows. 1. $Ca^{++}$ outflux from the resealed RBC was inhibited by suramin and the inhibitory action of suramin is proportional to the concentration of drug added inside the RBC preparation. When suramin is added both inside and outside the RBC preparation simultaneously, the magnitude of the inhibitory effect was more pronounced, suggesting that suramin inhibits both active $Ca^{++}-^{45}Ca$ exchange diffusion across the RBC membrane. 2. Suramin inhibits the $Ca^{++}$-activated ATPase of the RBCMF and the effect of inhibition by the drug was also concentration dependent. From the above results, it may be concluded that suramin inhibits $Ca^{++}$ transport across RBC membrane by inhibiting $Ca^{++}$-activated ATPase activity which has been known to be linked with active $Ca^{++}$ transport.

• 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.