• The Korean Journal of Food And Nutrition
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• v.17 no.2
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• pp.186-192
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• 2004

This study was performed to investigate softening methods of raw sea tangle for development of sea tangle processing products and intermediate materials. In examination of various softening agents, it was revealed that 0.3％ sodium triphosphate was best effective on softening with heat treatment. Softerness and spreadability of sea tangle treated with sodium triphosphate and heat treatment were indicated to be better than the others. In blanching studies, microwave was extremely effective on softening and the effect was as follows: microwave>steaming>boiling water in softening order. In the case of adding 0.3％ sodium triphosphate in blanching treatment, there was synergy effectiveness on softening. The color change of treated sea tangle was significantly different at p<0.05 depending on blanching method and addition amount of the agent.

• Archives of Pharmacal Research
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• v.16 no.1
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• pp.71-74
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• 1993

The protective effect of adenosine triphosphate (ATP) on gastic ulcer induced in rats has been studied. Gastic ulceration was induced by hypothemic restraint stress or dicolofenac sodium. Gastic acid secretion and mucosal injury produced by the hypothemic restraint stress was greater as compared with those produced by diclofenac sodifum. ATP significantly reduced area of injury, however, increased cyclic adenosine monophosphate (cATP) content. Administration of dipyridamole along with ATP did not change the total lesion area in both models when compared to ATP alone. Aminophyline antagonized antagonized the protective effect of ATP on the injured area. Famotidine was found to be effective in reducing gastric acid output as well as the total injured area without any change in cAMP content when given along with ATP.

• Microbiology and Biotechnology Letters
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• v.18 no.5
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• pp.471-475
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• 1990

A thermostable adenylate kinase isolated from the sonic extracts of Thermus caldophilus cells revealed higher substrate-specificity to the nucleoside monophosphate than to the nucleoside triphosphate. A $P', P^5$-di(adenosine-5') pentaphosphate was acted as a competitive inhibitor to the various substrates. Various divalent cations were activated the enzyme activity following orders: $Mg^{2+}, Ca^{2+}, Mn^{2+}, Ba^[2+}, $ and $Fe^{2+}$-. The enzyme activity was not affected by the sulfurhydryl reagent, p-chloromeric uribenzoic acid and activated by addition of the sodium chloride or phosphoenol pyruvate to the reaction mixture.

• Applied Chemistry for Engineering
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• v.29 no.6
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• pp.740-745
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• 2018

The synthesis and characterization of amorphous calcium phosphate (ACP) nanoparticles were reported in this work. We show that relatively monodisperse ACP nanoparticles with a size of sub-100 nm can be prepared by a hydrothermal reaction of calcium chloride ($CaCl_2$) and disodium adenosine triphosphate ($Na_2ATP$) in the presence of sodium phytate as an additive. Their compositions and structures were confirmed using a series of material characterization techniques. Our results exhibit that ACP nanoparticles synthesized using sodium phytate enhanced the stability of maintaining their amorphous nature and prevented from a conversion to crystalline hydroxyapatite (HAP). ACP nanoparticles with the improved stability have potential uses in biomaterial applications in regenerative medicine.

• Journal of Yeungnam Medical Science
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• v.7 no.1
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• pp.39-50
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• 1990

The one event on signalling mechanism is the cleavage by adenyl cyclase of ATP into second messenger, cyclic AMP. The other transfer system of inositol metabolism. it is widely recognized that hydrolysis of the minor membrane lipid phosphoinositide bisphosphate($PIP_2$) initiated by occupation of certain receptors and catalyzed by phospholipase C, lead to toe generation of the two intracellular messengers, inositol triphosphate($IP_3$) and diacylglycerol(DG). $IP_3$ is converted to inositol tetrakisphosphate($IP_4$) by $IP_3$ kinase. In the present study, it is that purification of calmodulin is used by phenyl-Sepharose CL-4B chromatography. it's molecular weigh, 17.000 in SDS-polyacrylamide gel electrophoresis. In order to observe the affinity between calmodulin (CaM)-Affigel 15 and $IP_3$ kinase, and isolated $IP_3$ kinase, was applied in CaM-Affigel with $Ca^{2+}$ equilibirum buffer and EGTA equilibirum buffer. We compared with binding and elution effect of $IP_3$ kinase in several condition of buffer. In affinity of binding. $Ca^{2+}$ equilibrium buffer was in the most proper condition. and elution, CaM/$Ca^{2+}$ buffer(CE1 10.36, CE2 12. 76pM/min/mg of protein) was effected much more than EGTA buffer(E2 1.48, E3 2.43pM/min/mg of protein), but CaM/$Ca^{2+}$ stimulate the activity of $IP_3$ kinase. And then, several detergents such as sodium deoxycholate, tween 20. cholic acid, polyethylene glycol, chaps were applied. The 0.2% chaps buffer(E2 23.19, E3 8.05pM/min/mg of protein) was the most effective in elution of $IP_3$ kinase.

• Animal cells and systems
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• v.7 no.2
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• pp.169-171
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• 2003

Sodium, potassium, calcium, zinc and magnesium levels in the serum of 31 patients diagnosed as acute myocardial infarction were analyzed on admission (within 24 Hours) and after 48 hours. The results were compared with those of 26 age matched controls. No significant difference was observed in the mean sodium, potassium, calcium and zinc levels between the cases and controls. Compared to the controls, however, the variation in the level of magnesium is highly significant at the time of admission as well as after 48 hours. When the risk factors like diabetes mellitus, hypertension, smoking and alcohol were considered, it is found that there is no significant difference between the risk groups as well as between the patients. The alteration in magnesium level in acute myocardial infarction is independent of these risk factors. Within the first 24 hours, the significant decrease in serum magnesium (35-51％ fall when compared with the control group), correlates with its entry into the cell following ischemia. From this hypomagnesemic state, it rises to 9-22 times after 48 hours. This hyper-magnesemia after 45 hours is probably due to the shift of magnesuim from the intracellular fluid compartment to the extracellular fluid compartment that follows cellular recovery. Therefore, including magnesium in the immediate management of acute myocardial infarction will be beneficial in the early recovery.

• Journal of Preventive Medicine and Public Health
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• v.25 no.1 s.37
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• pp.13-25
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• 1992

This study was conducted to investigate the mechanism of protective effect by sodium selenite in methylmercuric chloride neurotoxicity, increasing intracellular $Ca^{2+}$concentration of the neuron. Methylmercuric chloride of 3mg/kg of body weight was administered simultaneously with sodium selenite of 5mg/kg and pretreatment of sodium selenite via intraperitoneal injection to rats. Also, effect of methylmercuric chloride($25{\mu}M,\;50{\mu}M,\;100{\mu}M$) and sodium selenite($200{\mu}M$) on free intrasynaptosomal $Ca^{2+}$ concentration were studied using the fluorescent $Ca^{2+}$ indicator fura -2 in vitro. After the treatment, at 6, 24, and 48 hours later, mercury in the cerebral cortex, liver and kidney tissues, succlnic dehydrogenase activities, adenosin-5'-triphosphate concentration, acetylcholinesterase activities, and intracellular $Ca^{2+}$ concentration in the cerebral cortex were determined in vivo. Cerebral synaptosomes of rats were incubated with methylmercuric chloride and sodium selenite in Hepes buffer for 10 minutes and free intrasynaptosomal $Ca^{2+}$ concentration were measured with fura-2 in vitro. The results were summarized as follows ; 1. The combined administration of $CH_3HgCl$ and $Na_2SeO_3$ and pretreatment of $Na_2SeO_3$ according to time significantly more increased in the cerebral cortex and decreased in the liver, kidney mercury concentrations compared to the administration of $CH_3HgCl$ only. 2. The combined administration of $CH_3HgCl$ and $Na_2SeO_3$ and pretreatment of $Na_2SeO_3$ increased more succinic dehydrogenase and acetylcholinesterase activities compared to the administration of $CH_3HgCl$ only. Particularly pretreatment of $Na_2SeO_3$ significantly more compared to the administration of $CH_3HgCl$ only. The concentration of adenosine-5'-triphosphate in $Na_2SeO_3$ treatment groups revealed a favourable effect compared to the administration of $CH_3HgCl$ only. 3. Intracellular $Ca^{2+}$ concentration in administration of $CH_3HgCl$ only was increased significantly more than control group in all test hours but was increased significantly more at 48 hours only after treatment in combined administration of $CH_3HgCl$ and $Na_2SeO_3$ and pretreatment of $Na_2SeO_3$ according to time interval more decreased significantly intracellular $Ca^{2+}$ concentration compared to the administration of $CH_3HgCl$ only. 4. Free intrasynaptosomal $Ca^{2+}$ concentration in the combined administration of $CH_3HgCl$ and $Na_2SeO_3$ was decreased ($24%{\sim}40%$) significantly more than the administration of $CH_3HgCl$ only. From the above results, the specific dosage of $Na_2SeO_3$ decreased increment of intracellular $Ca^{2+}$ concentration induced by administration of $CH_3HgCl$. These findings suggest the protective mechanism of $Na_2SeO_3$ on the neurotoxicity of $CH_3HgCl$.

• BMB Reports
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• v.28 no.1
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• pp.72-78
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• 1995

Time-dependent inactivation of E. coli GTP cyclohydrolase I with a 2',3'-dialdehyde derivative of GTP (oGTP) was directed to the active site of the enzyme, and was dependent on the concentration of oGTP. The kinetics of inactivation were biphasic with a rapid reaction occurring immediately upon exposure of the enzyme to oGTP followed by a slow rate of inactivation. The $K_i$ value of oGTP for the enzyme was 0.25 mM. Inactivation was prevented by preincubation of the enzyme with GTP, the substrate of the enzyme. At 100% inactivation, 2.3 mol of [8.5'-$^3H$]oGTP were bound per each enzyme subunit, which consists of two identical polypeptides. The active site residue which reacted with the affinity label was lysine. oGTP interacted selectively with the ${\varepsilon}$-amino group of lysine in the GTP-binding site to form a morpholine-like structure which was stable without sodium borohydride treatment. However, triphosphate group was eliminated during the hydrolysis step. To identify the active site of the enzyme, [8.5'-$^3H$]oGTP-labeled enzyme was cleaved by endoproteinase Lys-C, and the $^3H$-labeled peptide was purified by HPLC. The amino acid sequence of the active site peptide was Pro-Ser-Leu-Ser-Lys, which corresponds to the aminoterminal sequence of the enzyme.

• Journal of Veterinary Science
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• v.23 no.5
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• pp.76.1-76.14
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• 2022

Background: Clinical dexamethasone (DEX) treatment or stress in bovines results in extensive physiological changes with prominent hyperglycemia and neutrophils dysfunction. Objectives: To elucidate the effects of DEX treatment in vivo on cellular energy status and the underlying mechanism in circulating neutrophils. Methods: We selected eight-month-old male bovines and injected DEX for 3 consecutive days (1 time/d). The levels of glucose, total protein (TP), total cholesterol (TC), and the proinflammatory cytokines interleukin (IL)-1β, IL-6 and tumor necrosis factor (TNF)-α in blood were examined, and we then detected glycogen and adenosine triphosphate (ATP) content, phosphofructosekinase-1 (PFK1) and glucose-6-phosphate dehydrogenase (G6PDH) activity, glucose transporter (GLUT)1, GLUT4, sodium/glucose cotransporter (SGLT)1 and citrate synthase (CS) protein expression and autophagy levels in circulating neutrophils. Results: DEX injection markedly increased blood glucose, TP and TC levels, the Ca²⁺/P⁵⁺ ratio and the neutrophil/lymphocyte ratio and significantly decreased blood IL-1β, IL-6 and TNF-α levels. Particularly in neutrophils, DEX injection inhibited p65-NFκB activation and elevated glycogen and ATP contents and SGLT1, GLUT1 and GR expression while inhibiting PFK1 activity, enhancing G6PDH activity and CS expression and lowering cell autophagy levels. Conclusions: DEX induced neutrophils glucose uptake by enhancing SGLT1 and GLUT1 expression and the transformation of energy metabolism from glycolysis to pentose phosphate pathway (PPP)-tricarboxylic acid (TCA) cycle. This finding gives us a new perspective on deeper understanding of clinical anti-inflammatory effects of DEX on bovine.

• The Korean Journal of Physiology
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• v.9 no.1
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• pp.1-11
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• 1975

The present experiments were carried out to investigate the active center of sodium and potassium ion activated adenosine triphosphatase. An ATPase, activated by sodium ion Plus potassium ion in the presence of magnesium ion, and inhibited by ouabain, has been obtained from rabbit red cell ghosts. The ATPase activity was measured by inorganie phosphate released from ATP. From this values of the measured inorganic phosphate, the activity of ATPase was calculated. The following results were observed. 1. The activity of $(Na^++K^+)-ATPase$ is inhibited by ouabain. This effect may not be due to an effect on sulfhydryl groups, amino groups, carboxyl groups, imidazole groups and hydroxyl groups. 2. The $(Na^++K^+)$-activated enzyme system is inhibited by p-chloromercuribenzoate and by d nitroflurobenzene, and this effect may be due to an effect on sulfhydryl groups. These results indicate that the sulfhydryl groups is attached to sodium-potassium dependent adenosine triphosphate, an aspect of the pump. 3. The $(Na^++K^+)-activated$ enzyme system is inhibited by maleic anhydride and this inhibition is reversed by lysine. This Seems to indicate that the active center of this enzyme is the amino groups. 4. The $(Na^++K^+)$-activated enzyme system is inhibited by iodoacetamide and this inhibition is reversed by the simultaneous present of cysteine and aspartic acid in the suspension medium. This result indicates that this enzyme contains sulfhydryl groups and carboxyl groups. 5. The $(Na^++K^+)-ATPase$ activity is accelerated by adrenaline and this effect is abolished by aspartic acid. This effect of aspartic acid indicate that carboxyl group might be involved in the hydrolysis of ATP by the enzyme system. On the hydrolysis of ATP by the enzyme system. On the basis of these experiments it f·as suggested that the active center of $(Na^++K^+)-activated$ ATPase contains sulfhydryl groups, amino groups and carboxyl groups.