• Toxicological Research
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• 제5권2호
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• pp.79-87
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• 1989

Changes in urinary $Na^+$ and $K^+$ excretions, renal cortical microsomal $Na^+$ -K-ATPase activity, cortical tissue electrolyte content and plasma aldosterone level were studied in rats treated with CdCl2 (2 mg Cd/kg/day, s.c. injection) for 7-14 days. After 7 days of cadmium exposure, urinary excretion of $Na^+$ was markedly reduced. This change was accompanied by an increase in $Na^+$-$K^+$-ATPase activity, a fall in tissue $Na^+$ content, a rise in tissue $K^+$ content and an elevation of plasma aldosterone level.

• The Korean Journal of Physiology
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• 제16권2호
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• pp.111-117
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• 1982

Slices of rat corpora lutea(CL) incubated with. prostaglandin $F_{{2{\alpha}}}(PGF_{2{\alpha}})$ in Krebs-Hensenleit (K-H) Ringer solution showed a decrease in $Na^+-K^+$-ATPase activity after 60 min of incubation. However, $PGF_{2{\alpha}}$ in vitro did not alter $Na^+-K^+$-ATPase activity of isolated luteal membrane fractions. Following $PGF_{2{\alpha}}$ induced in vivo luteal regression, reduction of Vmax an elevation of the activation energy above transition temperature of the lipid phase of the membrane occurred without changes of Km, optimum pH and transition temperature. These results suggest that reduction of $Na^+-K^+$-ATPase activity after $PGF_{2{\alpha}}$ treatment may be due to the reduction of the number of enzyme molecules or to masking of the active site of the enzyme without any change in enzyme characteristics. In addition, a change in membrane bound enzyme activity may be an early step in $PGF_{2{\alpha}}$ induced luleolysis.

• 한국균학회지
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• 제19권3호
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• pp.214-219
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• 1991

1. 표고버섯, L. edodes 중의 adenosine-5'-triphosphatase를 황산암모늄 30% 포화로 분별침전 및 Sephadex G-200 겔 여과로 정제하였다. 2. 이 버섯 중에는 3종류의 단백질 분획과 adenosine-5'-triphosphate 기질에 대한 두 종류의 활성분획 I, II, III 및 IV를 얻었다. 3. 활성분획 II를 정제하여 얻은 이 효소의 최적 pH 및 최적 온도는 각각 7.6 및 $58^{\circ}C$였고, 열 안정성은 $20-40^{\circ}C$에서 30분 동안 안정하였다. 이 효소의 Km값은 1.81mM이었다.

• Fisheries and Aquatic Sciences
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• 제8권1호
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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.

• 생약학회지
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• 제15권1호
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• pp.24-29
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• 1984

It was previously reported from our laboratory that the rate of deterioration of contractile force was slower in the heart of the ginseng extract treated rats. It was also found that ginseng may have an ability to sustain the normal function of the heart by sustaining Ca accumulation by sarcoplasmic reticulum. $Ca^{++}-dependent$ ATPase plays the central role in movement of $Ca^{++}$ ion from sarcoplasm into sarcoplasmic reticulum. In this investigation, the fragment of sarcoplasmic reticulum was prepared from rat heart treated with ginseng water extract orally 100mg/kg/day for 7 to 10 days and from normal rat heart. $Ca^{++}-dependent$ APTase activity was estimated by a modified method of Fiske and Subbarow's procedure. Experimental groups were divided into 6 groups, depending on the preincubation time, 5, 30 and 60min. at ${25}^{\circ}C$ and ${37}^{\circ}C$ respectively. In both of the groups of ${25}^{\circ}C$ and ${37}^{\circ}C$, $Ca^{++}-dependent$ ATPase activities of the ginseng treated rat hearts were higher than that of normal hearts. Therefore, it can be concluded that $Ca^{++}-dependent$ ATPase activities in sarcoplasmic reticulum of rat hearts were increased by the treatment with ginseng extract.

• 한국동물학회지
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• 제37권4호
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• pp.531-537
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• 1994

Partial internal amino acid sequences of the 15S ATPase from chick skeletal muscle were determined and found to be identical to the corresponding regions of the Mg2+_ATPase from Xenopus laevis oocytes, that is a close homolog of N-ethvlmaleimide-sensitive factor (called NSF) in hamster and Sec18p in yeast, both of which are believed to plaN an essential role in vesicle fusion in secretory process. Thus, the 15S Arpase in chick skeletal muscle maw also belong to a protein family of the "vesicle fusion proteins". Unlike the Mg2'-Afpase with an isoelectric point (pl) of 5.5, however, the 15S Arpase was separated into four spots with pls of 4.9,6.4 and 6.9 upon analysis by twoiimensional gel electrophoresis. In addition, the anti-15S ATPase IgG was found to be capable of interacting with the 265 protease complex upon analysis by immunoprecipitation. Moreover, immunoblot analysis revealed that the anti-155 Arpase IgG recognizes three subunits, ko of which show the same mobilities as the 510-kDa subunit 4 and 48-kDa subunit 7 of the 26S protease complex that are known to contain a highly consented ATP-binding motif. These results surest that a common antigenic site, likely the consensus nucleotide-binding site, exists in the 15S ATPase and the 26S pretense complex and hence both the enzymes maw also be related ATPases.d ATPases.

• The Korean Journal of Physiology
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• 제19권1호
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• pp.15-23
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• 1985

$(Na^++K^+)-ATPase$은 ${\alpha}$ 와 ${\beta}$의 두 subunits로 구성되어 있으며, 분자량이 약 300,000 daltons 정도되는 것으로 보아 ${\alpha}_2{\beta}_2$의 형태로 존재할 것으로 알려져 왔다 한편, 사람 적혈구막에 있는 $Na^+,\;K^+\;Pump$는 glycolytic enzymes과 complex를 이루고 있으리라는 보고도 있다. 우리는 이 실험에서 in situ상태의 사람 적혈구막$(Na^++K^+)-ATPase$의 분자량을 측정하기 위하여, 소위 말하는 ‘Target theory’를 radiation에 의한 ouabain sensitive한 $\Na^+$이동과, intact한 cells과 ghosts에서의 ATP가수분해능력의 inactivation data에 적용하였다. Intact한 cells은 cryoprotective agent의 존재하에서, ghosts는 직접적으로 액화질소의 용기속에 담고 온도를 $-45^{\circ}C$에서 $-50^{\circ}C$로 유지시키면서 1.5 MeV의 electron beam으로 조사한 후에 Pump의 기능내지 효소의 활성도를 측정하여 radiation에 따르는 inactivation의 정도를 측정하였다. 이득 활성도는 radiation의 양에 따라 simple exponential function으로 inactivation되었으며, 이로부터 radiation sensitive volume(target size)를 계산하였다. Target size는 intact한 cells을 사용하였을 경 우$(Na^++K^+)-ATPase$나 $Na^+,\;K^+\;Pump$ 모두 600,000 daltons으로 계산되었으며, 이 값은 만약 cells을 strophanthidin으로 먼저 처치하고 측정하면 약 325,000 daltons으로 감소하였다. Ghosts를 사용했을 경우에도$(Na^++K^+)-ATPase$의 target size는 역시 약 325,000 daltons이었다. 이상의 결과로 미루어 보아 intact한 cells에서는 $(Na^++K^+)-ATPase/Na^+,\;K^+\;Pump$가 $(\alpha\beta)_2$의 dimer 상태로 존재하거나 혹은 $(\alpha\beta)_2$의 monomer에 glycolytic enzymes과 같은 다른 enzymes이 붙어 functional한 구조를 이루고 있는 것이 아닌가 사료된다. 또한 실헐성적은 이러한 dimeric association 혹은 heterocomplex association은 ghost를 만드는 과정에서나 strophanthidin의 처치로 부서질 수 있음을 암시하고 있다.

• The Korean Journal of Physiology
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• 제22권2호
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• pp.163-177
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• 1988

세포막을 구성하고 있는 지질의 물리학적 성상이 단백질의 세포막 속으로의 삽입과정 및 단백질의 기능에 미치는 영향을 관찰하기 위하여 골격근의 근세망(SR)으로부터 $Ca^{2+}-ATPase$ 단백질을 분리한 후 이를 세포막의 주 구성성분인 포스파티딜콜린(PC)과 포스파티딜에타노라민(PE)의 혼합지질과 재조합(reconstitution)시켰다. 이와같이 인공적으로 재조합된 구조물에서 $Ca^{2+}-ATPase$의 기능을 측정하기 위하여 칼슘지시색소인 아르세나죠III(AIII)를 이용한 분광방법과 방사선동위원소를 이용한 여과법으로 칼슘흡수율을 측정하였고 또한 ATP 가수분해 능력을 측정하였다. 실험결과 칼슘의 흡수율은 포스파티딜코린의 함량이 많은 혼합지질과 재조합시킬 때에 증가하였고, ATP 가수분해 능력은 포스파티딜함량이 25%까지는 포스타피딜코린의 양에 비례하여 증가하였으나 50%이상에서는 약간 감소하는 경향을 보였다. 한편 지질세포막속으로 단백질이 삽입되는 양은 포스파티딜 함량이 25%일 때 최고의 값을 보였으며 함량이 그 이하 또는 이상일 때는 감소하였다. 이상의 실험결과로보아 단백질의 기능은 세포막이 "bilayer" 구조를 갖출때에 증가하고 세포막속으로 단백질이 삽입되는 양은 세포막이 "non-bilayer" 구조를 형성할 때에 증가함을 알 수 있다.

• 대한간호학회지
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• 제13권2호
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• pp.87-104
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• 1983

It has been well documented that animals exposed to cold show increased activity of thyroid gland. The calorigenic action of thyroid hormone has been demonstrated by a variety of in vivo and in vitro studies. According to Edelman et al., the thyroid thermogenesis is due to activation of energy consuming processes, especially the active sodium transport by the hormone in target tissues. If so, the increase in thyroid activity during cold exposure should induce increased capacity of sodium transport in target tissue and the change in tissue metabolism should be precisely correlated with the change in Na+_K+_ATPase activity of the tissue. This possibility was tested in the present study: in one series, changes in oxygen consumption and Na+_K+_-ATPase activity of liver preparations were measured in rats as a function of thyroid status, in order to establish the effect of thyroid hormone on the tissue respiration and enzyme system in another series, the effect of cold stimulus on the serum thyroid hormone level, hepatic tissue oxygen consumption and Na+_K+_ATPase activity in rats. The results obtained are as follows: 1. The Na+_dependent oxygen consumption of liver slices, the oxygen consumption of liver mitochondria and the Na+_K+_ATPase activity of liver preparations were significantly inhibited in hypothyroidism and activated in hyperthyroidism. Kinetic analysis indicated that the Vmax. of Na+_K+_ATPase was decreased in hypothyroidism and increased in hyperth)'roidism. 2. In cold exposed rats, the serum triiodothyronine (T₃) level increased rapidly during the initial one day of cold exposure, then declined slowly to the control level after two weeks. The serum thyroxine (T₄) level decreased gradually throughout the cold exposure. Accordingly the T₃/T₄ratio increased. The mitochondrial oxygen consumption and the Na+_dependent oxygen consumption of liver slices increased during the first two days and then remained unchanged thereafter The activity of the Na+_K+_ATPase in liver preparations increased during cold exposure with a time course similar to that of oxygen consumption. Kinetic analysis indicated that the Vmax. of Na+_K+_ATPase increased. 3. Once the animal was adapted to cold, induction of hypothyroidism did not significantly alter the hepatic oxygen consumption and Na+_K+_ATPase activity. These results indicate that: 1) thyroid hormone increases capacities of mitochondrial respiration and active sodium transport in target tissues such as liver; 2) the increased T₃level during the initial period of cold exposure facilitates biosynthesis of Na+_K+_ATPase and mitochondrial enzymes for oxidative phosphorylation, leading to enhanced production and utilization of ATP, hence heat production.

• 한국환경농학회지
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• 제20권1호
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• pp.28-33
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• 2001

본 시험에서 사용된 상추는 대조구인 양액과 양액에 30 mM $KNO_3$, 혹은 양액에 50 mM $KNO_3$를 첨가한 염류농도가 다른 3가지의 양액에서 재배하였으며 이들 양액의 EC는 각각 1.0, 4.5, 6.5 ds/m이었다. 상추의 생육은 처리간에 차이를 보였으며 $KNO_3$를 첨가하여 염류농도를 높여준 용액에서 재배한 상추는 잎끝이 마르는 생리적 장해를 보이면서 발아율의 감소는 물론 초장, 경태, 엽장 및 엽폭 등 성장이 대조구와 비교하여 현저히 부진하였다. 이들 양액에서 자란 상추의 뿌리로부터 마이크로솜을 분리하여 ATPase의 특성을 조사하였다. 마이크로솜 ATPase의 활성은 대조구에 비하여 양액에 30 mM $KNO_3$와 50 mM $KNO_3$를 첨가한 용액에서 자란 상추에서 더 높았다. 상추뿌리로부터 분리한 마이크로솜 ATPase의 총활성은 재배양액 조건에 관계없이 pH 7.0에서 최대로 나타났다. ATPase의 활성은 반응용액의 $K^+$ 농도를 증가시키면 증가하였고 반응용액에 $Na^+$ 농도를 증가시키면 감소하였다. $K^+$에 의한 활성증가 효과는 양액에서 재배한 대조구보다 $KNO_3$를 첨가하여 EC를 높여준 양액에서 재배한 상추뿌리의 마이크로솜 ATPase에서 더 크게 나타났다. 이러한 결과는 생육환경내 $KNO_3$ 농도의 증가에 따라 뿌리의 생리활성을 조절하는 ATPase의 활성이 증가함을 보여준다.