• Korean Journal of Food Science and Technology
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• v.20 no.3
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• pp.371-379
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• 1988

To investigate on the biochemical characteristics of myofibrillar proteins between cold(pollack, salmon) and warm current fish (yellow corbina, shark), myofibrils and actomyosin were prepared, and their biological activities, effect of temperature on the myofibrillar ATPase activities and SDS-polyacrylamide gel electrophoretic patterns of myofibrils were compared. SDS-polyacrylamide gel electrophoretic analysis showed that electrophoretic patterns of myofibril vary from fish to fish. Difference in KCl concentration dependency of myofibrillar ATPase activities and ATPase activity- pH curve were found among fish species. Myofibrillar proteins from cold current fish showed higher specific activity at low temperature $(5^{\circ}C-10^{\circ}C)$ than those from warm current fish.

• Journal of Microbiology and Biotechnology
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• v.8 no.3
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• pp.197-202
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• 1998

Aliphatic alkenals having 6 to 13 carbons were evaluated for antifungal activity against Saccharomyces cerevisiae. The activity was gradually increased with chain length, e.g., (E)-2-decenal and (E)-2-undecenal exhibited maximum potency, while (E)-2-dodecenal and (E)-2-tridecenal were completely inactive. Alkenals showed increasing inhibitory activity with chain length, as in the case of antifungal activity, towards glucose-induced medium acidification by the plasma membrane $H^+$-ATPase of S. cerevisiae. The group including (E)-2-nonenal, (E)-2-decenal, and (E)-2-undecenal exhibited maximum potency, but the potency of (E)-2-dodecenal and (E)-2-tridecenal demonstrated a sudden drop with respect to the former group. (E)-2-Nonenal revealed dose-responsive inhibition to the medium acidification and inhibited over 90% at a concentration of 1.25 mM ($175.3{\mu}g$/ml). In contrast to (E)-2-undecenal whose inhibitory efficiency increased with incubation time, inhibition by (E)-2-dodecenal was reversed with time. Of the tested alkenals, (E)-2-heptenal and (E)-2-octenal most highly inhibited ATP hydrolytic activity by the plasma membrane $H^+$ ATPase, while (E)-2-heptenal at 10 mM ($1121.8{\mu}g$/ml) showed an inhibitory efficacy of 93.2%.

• Journal of Physiology & Pathology in Korean Medicine
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• v.17 no.2
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• pp.542-548
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• 2003

The present study was aimed to investigate whether glycyrrhizin, which is the major component of Glycyrrhiza uralensis, has an antioxidant effect and regulatory effect on Na,K-ATPase in gentamicin-induced acute renal failure (ARF) rats . It is well known that reactive oxygen species (ROS), such as superoxide anion and hydroxyl radical, are main pathophysiological factor in gentamicin-induced ARF. Glycyrrhizin showed potent in vitro antioxidant activity, especially superoxide scavenging activity, in a dose-dependent manner. Plasma lipid peroxide level was restored to normal level by oral administration of glycyrrhizin (200 mg/kg) in the gentamicin-induced ARF rats. The expression of Na,K-ATPase α1 subunit was restored in the gentamicin-induced ARF rats by administration of glycyrrhizin, whereas β1 subunit was not restored. The renal functional parameters including urine volume, cleatinine clearance, urine osmolality, solute-free water reabroption were also partially restored in gentamicin-ARF rats by administration of glycyrrhizin. Taken together, the amelioration of renal functions and the expression of sodium pump by administration of glycyrrhizin in the gentamicin-induced ARF was appear to be mediated by the scavenging of ROS.

• Molecules and Cells
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• v.40 no.12
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• pp.925-934
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• 2017

The Cdc6 protein is essential for the initiation of chromosomal replication and functions as a licensing factor to maintain chromosome integrity. During the S and G2 phases of the cell cycle, Cdc6 has been found to inhibit the recruitment of pericentriolar material (PCM) proteins to the centrosome and to suppress centrosome over-duplication. In this report, we analyzed the correlation between these two functions of Cdc6 at the centrosome. Cdc6 depletion increased the population of cells showing centrosome over-duplication and premature centrosome separation; Cdc6 expression reversed these changes. Deletion and fusion experiments revealed that the 18 amino acid residues (197-214) of Cdc6, which were fused to the Cdc6-centrosomal localization signal, suppressed centrosome over-duplication and premature centrosome separation. Cdc6 mutant proteins that showed defective ATP binding or hydrolysis did not exhibit a significant difference in suppressing centrosome over-duplication, compared to the wild type protein. In contrast to the Cdc6-mediated inhibition of PCM protein recruitment to the centrosome, the independence of Cdc6 on its ATPase activity for suppressing centrosome over-duplication, along with the difference between the Cdc6 protein regions participating in the two functions, suggested that Cdc6 controls centrosome duplication in a manner independent of its recruitment of PCM proteins to the centrosome.

• The Korean Journal of Physiology
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• v.17 no.1
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• pp.55-61
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• 1983

Effects of SITS (4-acetamido-4'-isothiocyano-2, 2'-disulfonic stilbene) on a $Na^+$ transport, tissue oxygen consumption and Na-K-ATPase activity were studied in isolated frog skin preparations. $Na^+$ transport was estimated by measuring the short-circuit current(SC) across the skin; oxygen consumption was measured in separated epidermis as well as in intact skin; and Na-K-ATPase was assayed in $24,000{\times}g$ fraction of epidermal homogenates. The SCC across the skin Was rapidly and substantially reduced in the presence of 10 mM SITS in the medium bathing the outside(mucosal) surface of the skin. When the drug was added to the inside(serosal) bathing medium, there was about 20 min delay for inhibition of SCC and the effect was less pronounced. The above effect of SITS was independent of the presence of $Cl^-$ in the bathing medium. The oxygen consumption of the skin tissue was not affected by SITS, but the Na-K-ATPase activity of a subcellular fraction of the skin was significantly inhibited. These results suggest that SITS retards $Na^+$ transport across the frog skin primarily by interfering $Na^+$ entry across the mucosal membrance of the epithelial cell, although an effect on $Na^+$ pump can not be ruled out completely.

• The Korean Journal of Physiology
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• v.18 no.2
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• pp.139-150
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• 1984

Vanadate is a potent inhibitor of Na-K-ATPase. Ouabain, the another specific inhibitor of Na-K-ATPase, induces the contraction in cardiac muscle and smooth muscle. But, some investigators observed the discrepancies between vanadate and ouabain-induced contraction in cardiac muscle. The difference of vanadate and ouabain-induced contraction was investigated in the cat ileal smooth muscle. The following results were obtained. 1) Ouabain-induced contraction was biphasic, but vanadate-induced contraction had one peak. 2) Atropine inhibited ouabain·induced contraction, but did not inhibit vanadate-induced contraction. 3) Changes in external $Ca^{++}$concentration or $Ca^{++}$ antagonists had a greater influence on the contraction induced hy vanadate than by ouabain. 4) Removal of $Na^+$ from incubation medium and high $K^+$ abolished ouabain-induced contraction, but had no effect on vanadate-induced contraction. 5) Vanadate-induced contraction was potentiated in the presence of ouabain. 6) After 3 hrs incubation with vanadate, there was no change in intracellular $Na^+$ concentrations in contrast with ouabain. These results suggest that vanadate contracts ileal smooth muscle through the mechanism different from ouabain, and this is independent of the inhibition of Na-K-ATPase activity.

• Korean Journal of Microbiology
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• v.43 no.4
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• pp.250-255
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• 2007

The RecA protein of Deinococcus radiodurans is essential for the extreme radiation resistance of this organism. The central steps involved in recombinational DNA repair require DNA-dependent ATP hydrolysis by recA protein. Key feature of RecA protein-mediated activities is the interactions with ssDNA and dsDNA. The ssDNA is the site where RecA protein filament formation nucleates and where initiation of DNA strand exchange takes place. The effect of sequence heterogeneity of ssDNA was examined in this experiment. The rate of homopolymeric synthetic ssDNA-dependent ATP hydrolysis was constant or nearly so over a broader range of pHs. For poly(dT)-dependent ATP or dATP hydrolysis, rates were generally faster, with a broader optimum between pH 7.0 and 8.0. Activities of RecA protein were affected by the ionic environment. The ATPase activity was shown to have different sensitivity to anionic species. The presence of glutamate seemed to slimulate the hydrolytic activity. Dr RecA protein was shown to require $Mg^{2+}$ ion greater than 2 mM for binding to etheno ssDNA and the binding stoichiometry of 3 nucleotide for RecA protein monomer.

• Journal of the Korean Society of Food Science and Nutrition
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• v.16 no.3
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• pp.55-61
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• 1987

This study was carried out to investigate the changes in the pH, extractability of protein, ATPase activity of myofibrillar protein, myofibrillar fragmentation, freezing loss and drip loss during storage at $4^{\circ}C$ and $-20^{\circ}C$ in breast and leg muscle of spent-hen meat. pH values ill pectoral and leg muscle were lowest ell tile 1st day and 1st week during cold and frozen storage, respectively. The extractabilities of myofibrillar proteins were increased graduall during cold storage and were highest on the 1st week during frozen storage, The $Mg^{2+}-ATPase$ activities of myofibrillar proteins were highest on the 1st day and 1st week during cold and frozen storage, respectively. The myofibrillar fragmentations were greatly changed on the 1st day during cold storage and 1st week during frozen storage. Freezing losses and drip losses were increased gradually during frozen storage. pH values in breast muscle were lower than those of leg muscle, and the extractabilities, $Mg^{2+}-ATPase$ activities, fragmentations of myofibrillar proteins, and drip losses in breast muscle were higher than those of leg muscle during storage, but the patterns of the changes in both muscles were similar during storage.

• Asian-Australasian Journal of Animal Sciences
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• v.33 no.7
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• pp.1077-1086
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• 2020

Objective: We examined the localization and expression of H⁺ pumping vacuolar ATPase (V-ATPase) and cytokeratin 5 (KRT5) in the epididymis of pigs, expressed in clear and basal cells, respectively, during postnatal development. Methods: Epididymides were obtained from pigs at 1, 7, 21, 60, 120, and 180 days of age; we observed the localization and expression patterns of V-ATPase and KRT5 in the different regions of these organs, namely, the caput, corpus, and cauda. The differentiation of epididymal epithelial cells was determined by immunofluorescence labeling using cell-type-specific markers and observed using confocal microscopy. Results: At postnatal day 5 (PND5), the localization of clear cells commenced migration from the cauda toward the caput. Although at PND120, goblet-shaped clear cells were detected along the entire length of the epididymis, those labeled for V-ATPase had disappeared from the corpus to cauda and were maintained only in the caput epididymis in adult pigs. In contrast, whereas basal cells labeled for KRT5 were only present in the vas deferens at birth, they were detected in all regions of the epididymis at PND60. These cells were localized at the base of the epithelium; however, no basal cells characterized by luminally extending cell projections were observed in any of the adult epididymides examined. Conclusion: The differentiation of clear and basal cells progressively initiates in a retrograde manner from the cauda to the caput epididymis. The cell-type-specific distribution and localization of the epithelial cells play important roles in establishing a unique luminal environment for sperm maturation and storage in the pig epididymis.

• The Korean Journal of Physiology and Pharmacology
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• v.16 no.2
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• pp.91-95
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• 2012

The role of the kidney in combating metabolic acidosis has been a subject of considerable interest for many years. The present study was aimed to determine whether there is an altered regulation of renal acid base transporters in acute and chronic acid loading. Male Sprague-Dawley rats were used. Metabolic acidosis was induced by administration of $NH_4Cl$ for 2 days (acute) and for 7days (chronic). The serum and urinary pH and bicarbonate were measured. The protein expression of renal acid base transporters [type 3 $Na^+/H^+$ exchanger (NHE3), type 1 $Na^+/{HCO_3}^-$ cotransporter (NBC1), Na-$K^+$ ATPase, $H^+$-ATPase, anion exchanger-1 (AE-1)] was measured by semiquantitative immunoblotting. Serum bicarbonate and pH were decreased in acute acid loading rats compared with controls. Accordingly, urinary pH decreased. The protein expression of NHE3, $H^+$-ATPase, AE-1 and NBC1 was not changed. In chronic acid loading rats, serum bicarbonate and pH were not changed, while urinary pH was decreased compared with controls. The protein expression of NHE3, $H^+$-ATPase was increased in the renal cortex of chronic acid loading rats. These results suggest that unaltered expression of acid transporters combined with acute acid loading may contribute to the development of acidosis. The subsequent increased expression of NHE3, $H^+$-ATPase in the kidney may play a role in promoting acid excretion in the later stage of acid loading, which counteract the development of metabolic acidosis.