• Journal of Nutrition and Health
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• 제30권2호
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• pp.170-176
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• 1997

Twenty two hypertensive and thirty normotensive in-patients were participated in this study to investigate the relationship between plasma renin activity and metabolism of Ca and Na, Prior to pharmacological treatments, renin activity, aldosterone and parathyroid hormone(PTH) levels were measured from the fasting blood samles. Twenty four hour urine samples were collected to analyze urinary levels of creatinine, Ca, Na and K. Habitual intake of Na and Ca were also measured for hypertensive and normotensive patients. Hypertensive subjects were classified into higher reinin hypertensive (HH), medium renin hypertensive(MH) and low renin hypertensive (LH) group according to their renin activities. PTH level of LH group was the highest among three hypertensive groups. It appeared that aldosterone levels of HH group were significantly higher than LH or MH groups(p<0.05). However there were no significan시 differences in aldosterone level between LH group and normotensive group. Habitual intake of Na and Ca were highest in LH group but lowest in HH group, however, they were not statistically different. Positive correlations of systolic blood pressure with PTH(r=0.2597) and aldosterone(r=0.26480existed(p<0.05). Urinary Ca level was positively correlated with urinary Na(r=0.5619), K(r=0.4533) and habitual Na intake(r=0.3253). Above results suggested the possible relationships among renin activity, habitual Ca intake and Na intake and suggested a further study on the interrelationship between the hormonal control of Ca and Na metabolism and blood pressure in hypertension.

• Archives of Pharmacal Research
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• 제12권2호
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• pp.128-134
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• 1989

$Na^+-Ca^{2+}$ exchange process in sarcolemmal vesicles isolated from mesenteric arteries of Wistar-Kyoto normotensive(WKY) and spontaneously hypertensive rats(SHR) was investigated. The sarcolemmal fractions isolated after homogenization and sucrose density gradient centrifugation were enriched with 5'-nucleotidase and ouabain sensitive, $K^+-dependent$ phosphatase activities. When the vesicles were loaded with $Na^+$, a time dependent $Ca^{2+}$ uptake was observed. However, very little $Ca^{2+}$ uptake was observed when the vesicles were loaded with $K^+$, or $Ca^{2+}$ uptake of the $Na^+-loaded$ vesicles was carried out in high sodium medium so that there was no sodium gradient. When the vesicles loaded with $Ca^{2+}$ by $Na^+-Ca^{2+}$ exchange were diluted into potassium medium containing EGTA, $Ca^{2+}$ was rapidly released from the vesicles. $Na^+-dependent\;Ca^{2+}$ uptake was increased in SHR compared to WKY, but passive efflux of preaccumulated $Ca^{2+}$ from the vesicles was decreased in SHR. The data indicate that the membrane vesicles of rat mesenteric arteries exhibit $Na^+-Ca^{2+}$ exchange activity. It is also suggested that changes of this process in vascular smooth muscle cell membrane of SHR may be involved in higher intracellular $Ca^{2+}$ concentration and higher basal tone in SHR.

• BMB Reports
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• 제42권10호
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• pp.642-647
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• 2009

In this study, the effects of $Ca^{2+}$ and cyclic adenosine monophosphate (cAMP) on microsomal triglyceride (TG) transfer protein (MTP) activity were investigated in rat liver. MTP activity was high when liver contained low levels of cAMP, which was induced by administration of glucose, or high levels of total $Ca^{2+}$ and TG. However, MTP activity increased by high levels of $Ca^{2+}$ and TG was reduced in a dose-dependent manner by treatment with dibutyryl-cAMP (db-cAMP), a cAMP analogue. Conversely, when homogenates of liver from normal rats, with low levels of total $Ca^{2+}$ and high levels of cAMP, were incubated with thapsigargin, a $Ca^{2+}$-inducer, MTP activity was increased in a dose-dependent manner compared to control. Therefore, our results suggest that high levels of $Ca^{2+}$ cause hypertriglyceridemia through the elevation of MTP activity, as opposed to high levels of cAMP, which suppress MTP activity and inhibit hypertriglyceridemia.

• 한국수산과학회지
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• 제31권4호
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• pp.545-552
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• 1998

생선회의 육질을 향상시키는 연구의 일환으로 어육에 있어서 전기자극에 의한 근수축의 증대원인을 밝히고자 전기자극처리가 근소포체의 특성에 미치는 영향을 살펴보았다. 넙치 근소포체의 $Ca^{2+}$-ATPase는 $50^{\circ}C$ 이상의 온도에서 실활되었으며, 전기자극시킨 경우 즉살한 것에 비하여 낮은 $Ca^{2+}$-ATPase활성을 나타내었다. 근육을 $5^{\circ}C$에 저장하였을때 시간이 길어질수록 근소포체의 $Ca^{2+}$-ATPase는 치사직후에 비하여 저하되는 경향을 보였으며, 전기자극 시간이 길어질수록 빠르게 저하되었고. 35초와 60초간 전기 자극시킨 것은 비슷한 저하속도를 나타내었다. SDS-PAGE 결과, 97kDa과 68kDa의 성분이 주된 구성단백질이었으며. 전기자극 시킨것은 즉살시킨 것에 비하여 97kDa의 성분이 감소되었고 전기자극 시간이 길어질수록 현저하였다. LSR은 $27\~32\%$ sucrose 농도에서, HSR은 $38\~45\%$의 농도에서 얻을 수 있었다. LSR의 $Ca^{2+}$-ATPase는 전기자극에 의하여 실활되었으며, HSR은 큰 영향을 받지 않았다 근원섬유의 $Mg^{2+}$-ATPase 활성은 전기자극처리에 의하여 증가되었으며 자극시간이 길어질수록 저장 중 $Mg^{2+}(+Ca^{2+}$)-ATPase 활성의 저하는 즉살한 것에 비하여 빠르게 진행되었다. $Mg^{2+}(-Ca^{2+}$)-ATPase 활성의 변화는 $Mg^{2+}(+Ca^{2+}$)-ATPase 활성과 비슷한 경향을 나타내었으며, 전기자극한 것은 저장 중 저하되었으나 즉살한 것은 치사 직후와 비교하여 큰 차이를 나타내지 않았다. 근원섬유의 $Ca^{2+}$-감수성은 즉살과 전기자극한 것 사이에 차이를 나타내지 않았으며, 저장 중에도 변화를 보이지 않았다.

• Fisheries and Aquatic Sciences
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• 제17권3호
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• pp.291-298
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• 2014

We investigate the effects of cryoprotectant mixtures on the quality of sand lance surimi (SLS) during storage at $-30^{\circ}C$. We monitored freeze-induced denaturation of myofibrillar protein in SLS and examined the texture profile of SLS gel. Freeze-induced denaturation was assessed by evaluating SLS $Ca^{+2}$-ATPase activity. SLS gels prepared with sorbitol or sucrose and a mixture of both as cryoprotectant. Higher concentrations of cryoprotectants resulted in significantly higher residual SLS $Ca^{+2}$-ATPase activity at the same storage time (P < 0.05). Residual $Ca^{2+}$-ATPase activity of SLS prepared with sorbitol was higher than that of sucrose when cryoprotectant concentration and storage period were same. A blend of sorbitol and sucrose resulted in a stronger cryoprptective effect of SLS myofibrillar protein than did sorbitol or sucrose alone. The presence of a phosphate compound in SOP (3% sorbitol + 0.2% phosphate compound) resulted in higher SLS $Ca^{2+}$-ATPase activity than that of did 5% sorbitol. The hardness, brittleness, and elasticity values and a folding test of the SLS gels were significantly affected by cryoprotectant concentrations and the storage time. Preference scores and acceptance for texture in a sensory evaluation of the SLS gels increased with increasing sorbitol or sucrose concentration.

• 한국식품영양과학회지
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• 제19권4호
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• pp.349-355
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• 1990

Actomyosine prepared from Yellowtail fish(seriola quinqueradiata) were stored at $0^{\circ}C$(ice-cooling) -3.5$^{\circ}C$(partial freeaing) and -2$0^{\circ}C$(freezing) Another actomyosin samples were prepared from the fish previously stored at the temperatures for a week as the maximum .Remaining activity of {{{{ {Ca }^{2+ } }}}}-and {{{{ {Mg }^{2+ } }}}}- dependent adenosine triphosphatase(ATPase) activity was measured fronm the actomyosin preparations. Specific activity of {{{{ {Mg }^{2+ } }}}}-ATPase of actomy-osin before storagew was 0.253$\mu$ mole pi/min/mg of protein and it was 1.5 times higher than that of {{{{ {Ca }^{2+ } }}}} -ATPase. The enzyme activities were markedly decreased during early period of storage. However no significant differences in the enzyme activity were revealed among the samples stored at different temperature. The enzyme of actomyosin prepared from the fish previously stored at the temperatures for a week revealed an acitivity of 2-3 times higher than that of freezing. Apparent denaturation constant of {{{{ {Mg }^{2+ } }}}} -ATPase of actomyosin was between 0.810-1.139 per day and it was about 1.5 times hgiher than that of {{{{ {Ca }^{2+ } }}}} -ATPase. But the constant of {{{{ {Mg }^{2+ } }}}} ATPase of actomyosin extracted from the fist stored for a week at each temperature was between 0.176-0.356 per day. This constant was 4 times higher than that of {{{{ {Ca }^{2+ } }}}}- ATPase in frozen stored fish. It was presumed from these results that denaturation of ATPase is largely accorded to the structural changes of actomyosin.

• 한국결정성장학회지
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• 제33권5호
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• pp.187-190
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• 2023

본 연구에서는 ZnO-Na₂O-B₂O₃-SiO₂ 계 유리에 CaO의 첨가에 따른 유리의 열적, 화학적 특성, 표면 제타전위 및 항균특성을 분석하였다. 유리 조성에 따른 열적 특성은 DTA 분석을 통해 확인하였고, 30ZnO-xCaO-20Na₂O-30B₂O₃-(20-x)SiO₂ (x = 0, 2, 4, 6, 8, 10 mol%)계 유리에서 CaO 함량이 증가함에 따라 유리전이온도가 줄어드는 것을 확인하였다. CaO 함량이 늘어날수록 유리 구조가 약화됨에 따라 더 많은 Zn²⁺ 이온이 용출되었고, 알칼리 및 알칼리 토류의 초기 급속한 용출로 인해 유리의 표면 제타전위가 증가함을 확인하였다. 이러한 이유로 유리의 항균활성 또한 급격하게 개선됨을 확인하였으며, 대장균(gram negative)과 황색포도상구균(gram positive) 모두에 대해 99.9 % 항균 활성을 갖는 항균 유리를 개발할 수 있었다.

• Journal of Microbiology
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• 제35권1호
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• pp.21-24
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• 1997

The hybrid peptides, CA-ME, CA-MA and CA-BO, with the N-terminal sequence 1-8 of cecropin A and the N-terminal sequences 1-12 of melittin, magainin 2 and bombinin, respectively, have more improved antibacterial activities. CA-MA was found to have stronger antifungal activity against Trichoderma sp than other hybrid peptides and their parental peptides. In order to elucidate the relationships between the peptide structure and antifungal activity, several analogues of CA-MA or CA-BO were also designed and synthesized by the solid phase method. An tifungal activity was measured against T. reesei and T. viride, and hemolytic activity was measured by a solution method against human red blood cells. The residue 16 of CA-MA, Ser, was found to be important for antifungal activity. When the residue was substituted with Leu, showed powerful antifungal activity was dramatically decreased. CA-MA, P1, P4 and P5 designed in this study showed powerful antifungal activity against T. reesei and T. viride with low hemolytic activity against human red blood cells. These hybrid peptides will be potentially useful model to further design peptides with powerful antifungal activity for the effective therepy of fungal infection and understand the mechanisms of antifungal actions of hybrid peptides.

• 동아시아식생활학회지
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• 제15권5
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• pp.598-605
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• 2005

Effects of chitosan-ascorbate(CA) and calcium lactate(CL) on fermentation and quality of squid sikhae were investigated CA and LA were added at $0.5\%$ (designated CA1 and CL1) and $1.0\%$(CA2 and CL2) concentrations, respectively and fermented for 12 days at $10^{\circ}C$. pH of CA-added sikhae was higher than that of control, while acidity of the former was lower than that of the latter. During 12 days of fermentation, CA-added sikhae showed higher protease activity than control by $2.3\~2.6$ times and CL-added sikhae by $2.8\~3.6$ times. At 12 days of fermentation, CA-added sikhae revealed higher protease activity than control by $1.2\~1.4$ times and CL-added sikhae by $1.5\~1.9$ times. CA-added sikhae also showed higher amino-nitrogen content than control by $1.4\~1.7$ times and CL-added sikhae by $1.9\~3.5$ times. In comparison of CA1 with CA2, CA2 showed all higher pH, protease and amylase activity, and amino-nitrogen content than CA1. In analysis of electrophoresis, molecular weights of major proteins in ~w squid were $116.9\~119.0$, 96.5 and 59.3kDa. However, after fermentation for 12 days, a protein band of 119.0kDa disappeared but a new protein band with below 14 kDa appeared in sikhae, especially CA-added sikhae. In sensory evaluation, the intensity of sour taste was the highest for control and the lowest for CA2. Softness of squid was the highest for control and the lowest for CA2. Overall acceptability was the best for CA2. In conclusion, these results suggest use of $1\%$ CA in sikhae preparation as addition of CA(CA2) increased the protease and amylase activity, nitrogen content of amino form, sensory acceptability as well as shelf-life of sikhae.

• The Korean Journal of Physiology and Pharmacology
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• 제9권4호
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• pp.203-207
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• 2005

Electrical rhythmicity in the gastrointestinal (GI) muscles is generated by pacemaker cells, known as interstitial cells of Cajal (ICC). In the present study, we investigated the effect of external divalent cations on pacemaking activity in cultured ICC from murine small intestine by using whole-cell patch clamp techniques. ICC generated pacemaker currents under a voltage clamp or electrical pacemaker potentials under a current clamp, and showed a mean amplitude of $-500{\pm}50$ pA or $30{\pm}1$ mV and the frequency of $18{\pm}2$ cycles/min. Treatments of the cells with external 0 mM $Ca^{2+}$ stopped pacemaking activity of ICC. In the presence of 2 mM $Ca^{2+}$, 0 mM external $Mg^{2+}$ depolarized the resting membrane potential, and there was no change in the frequency of pacemaking activity. However, 10 mM external $Mg^{2+}$ decreased the frequency of pacemaking activity ($6.75{\pm}1$ cycles/min, n=5). We replaced external 2 mM $Ca^{2+}$ with equimolar $Ba^{2+}$, $Mn^{2+}$ and $Sr^{2+}$, and they all developed inward current in the sequence of $Ba^{2+}$>$Mn^{2+}$>$Sr^{2+}$. Also the frequency of the pacemaking activity was stopped or irregulated. We investigated the effect of 10 mM $Ba^{2+}$, $Mn^{2+}$ and $Sr^{2+}$ on pacemaking activity of ICC in the presence of external 0 mM $Mg^{2+}$, and found that 10 mM $Ba^{2+}$ and $Mn^{2+}$ induced large inward current and stopped the pacemaking activity of ICC (n=5). Interestingly, 10 mM $Sr^{2+}$ induced small inward current and potentiated the amplitude of pacemaking activity of ICC (n=5). These results indicate that extracellular $Ca^{2+}$ and $Mg^{2+}$ are requisite for the pacemaking activity of ICC.