• Title/Summary/Keyword: $\alpha$-D- and $\beta$-D-mannosidase

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Effects of Intravenous Administration of Taurocholic Acid on Liver Lysosomal $\alpha$-D- and $\beta$D-Mannosidase Activities in Rats with Extrahepatic Cholestasis

  • Park, So-Kyung;Kim, You-Hee;Kwak, Chun-Sik
    • Biomedical Science Letters
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    • v.10 no.2
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    • pp.93-98
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    • 2004
  • The effects of intravenously administered of high concentration of taurocholic acid (TCA) on $\alpha$-D- and $\beta$-D-mannosidase activities in rat liver lysosomes were studied. These liver lysosomal enzymes, and serum lysosomal $\alpha$-D- and $\beta$-D-mannosidase isozymes activities were determined in experimental rats with common bile duct ligation (CBDL). The liver lysosomal $\beta$-D-mannosidase activity as well as the serum lysosomal $\alpha$-D- and $\beta$-D-mannosidase isozymes activities were found to be significantly increased in the CBDL plus TCA injected group than in the control group such as CBDL alone group. However, the liver lysosomal $\alpha$-D-mannosidase activity was found to be significantly decreased in the CBDL plus TCA injected group. The above results suggest that TCA repress the biosynthesis of the lysosomal $\alpha$-D-mannosidase and induce the biosynthesis of the lysosomal $\beta$-D-mannosidase in the liver. And that the elevated serum lysosomal $\alpha$-D- and $\beta$-D-mannosidase isozymes activities are most likely due to increased hepatocyte membrane permeability caused by TCA mediated liver cell necrosis.

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Exo-O-Glycosylhydrolases in Korea Ginseng Roots

  • Yelena V.Sundukova;Lee, Mi-Ja;Park, Hoon
    • Journal of Ginseng Research
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    • v.24 no.2
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    • pp.89-93
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    • 2000
  • WB were screening the stele and the cortex of the ginseng roots (Panax ginseng C.A.Meyer) on the exo-0-glycosylhydrolase activities during vegetation period of 1999 year. The following p-nitrophenylglycosides were used to test exe-0-glycosylhydrolase activities: $\alpha$- and $\beta$-D-galactopyranosides,$\alpha$- and $\beta$-D-glucopyranosides, $\alpha$- and $\beta$-D-mannopyranosides, N-acetyl-$\beta$-D-glucosaminide, $\alpha$- and $\beta$-D-xylopyranosides $\alpha$- L-rhamnopyranoside, $\beta$-D-glucuronide, $\beta$-D-galacturonide, $\beta$-L-,$\alpha$-L- and $\beta$-D-fucopyranosides, $\alpha$-L-arabinopyranoside. Only $\beta$-D-galactosidase, $\alpha$-L-mannosi-dase , N- acetyl- ${\beta}$-D-slucosarninidase, $\alpha$-D-galacto sidase, $\alpha$-L-arabinosidase, and $\beta$-D-fuco sidase were found in both partsof ginseng roots. Their contents during the vegetation period were shown to differ considerably, being dependent not only on plant development stage but on plant tissue and environmental conditions too.

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Mannanolytic Enzyme Activity of Paenibacillus woosongensis (Paenibacillus woosongensis의 만난분해 효소활성)

  • Yoon, Ki-Hong
    • Korean Journal of Microbiology
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    • v.46 no.4
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    • pp.397-400
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    • 2010
  • The activities of mannanase, ${\beta}$-mannosidase, and ${\alpha}$-galactosidase were detected in culture filtrate of Paenibacillus woosongensis showing mannanolytic activity for locust bean gum. Optimal conditions occurred at pH 5.5 and $60^{\circ}C$ for mannanase toward locust bean gum, pH 6.5 and $50^{\circ}C$ for ${\beta}$-mannosidase toward para-nitrophenyl-${\beta}$-D-mannopyranoside, and pH 6.0-6.5 and $50^{\circ}C$ for ${\alpha}$-galactosidase toward para-nitrophenyl-${\alpha}$-D-galactopyranoside in the culture filtrate, respectively. The mannanolytic enzyme of culture filtrate hydrolyzed mannobiose as well as manno-oligosaccharides including mannotriose, mannotetraose, mannopentaose and mannohexaose. It could also hydrolyze ${\alpha}$-1,6 linked galacto-oligosaccharides such as melibiose, raffinose and stachyose to liberate galactose residue. From these results, it is assumed that P. woosongensis produces three enzymes required for the complete decomposition of galactomannan.

Changes of Glycosidase Activity and Fertilizing Ability in Vitro by Incubation of Frozen-Thawed Spermatozoa in the Pig (돼지 동결정액의 배양에 따른 체외수정능력과 Glycosidase Activity의 변화)

  • 황인선;정희태;양부근;김정익;박춘근
    • Korean Journal of Animal Reproduction
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    • v.27 no.2
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    • pp.153-161
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    • 2003
  • This study has evaluated effect of the spermatozoa incubation on the glycosidase activity and fertilizing ability in vitro in the pig. To identify sperm glycosidases specific for sugar residues found in the zona pellucida of pig oocytes, the spermatozoa were treated experimentally and assayed for activities of $\alpha$-L-fucosidase, $\alpha$-D-mannosidase, $\beta$-D-galactosidase and N-acetyl-$\beta$-D-glucosaminidase ($\beta$-GlcNAc'ase). The glycosidases activity were higher in spermatozoa incubated for 2h than without incubation. The $\beta$-GlcNAc'ase activity was at least two-fold higher than other glycosidase regardless of spermatozoa incubation. In the same glycosidases, the activity had a tendency to increase as time of spermatozoa incubation was prolonged, but there were no differences in spermatozoa incubated during the various periods (4~24h). The percentages of spermatozoa that reached acrosome reaction were affected by glycosidases in the medium (P<0.05, for mannosidase), and were higher in spermatozoa with that than without incubation. On the other hand, the spermatozoa motility were decreased with incubation periods, but no effects by different glycosidases on the change of sperm motility during the various periods of incubation. In other experiment, the binding and penetration of pig spermatozoa were tested with oocytes matured in vitro in the presence of various glycosidase. The penetration rates were decreased with incubation of spermatozoa when oocytes were inseminated in medium with different glycosidases. These rates were higher in spermatozoa non-incubated than with incubation for 2h (P<0.05 for GlcNAc'ase; P<0.01 for control group). The sperm-zona binding rate in control group were higherthan in medium with glycosidases. In addition, the highest binding rate were obtained in medium with GlcNAc'ase. In all glycosidases, the sperm-zona binding rate in spermatozoa without incubation were higher than incubation for 2h. The significant differences were obtained in spermatozoa treated with $\alpha$-D-mannosidase (P<0.05). These results suggest that $\beta$-GlcNAc'ase is present mainly in the plasma membrane of pig spermatozoa. It was also shown that the glycosidase activity were increased in all glycosidases in spite of low sperm-zona binding rate and penetration rates by spermatozoa incubation.

Purification and Characterization of an α-D-Galactosidase from Grape Berry

  • Kang, Han-Chul;Kim, Tae-Su
    • Journal of Applied Biological Chemistry
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    • v.43 no.3
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    • pp.141-146
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    • 2000
  • Glycosidase activities were tested from the grape berries, Vitis labruscana B. Takasumi. Among various glycosidases, $\alpha$-D-galactosidase was found to be the most active in the flesh and other glycosidases were considerably active in the order of the following: $\alpha$-D-mannosidase>$\alpha$-D-glucosidase>$\beta$-D-glucosidase>$\beta$-D-galactosidase. In the seeds, $\alpha$-D-glucosidase activity was the highest and other glycosidases such as $\alpha$-D-galactosidase, $\beta$-D-glucosidase, and $\beta$-D-galactosidase were still significantly active. The $\alpha$-D-galactosidase in the grape flesh was purified over 83-folds through salting-out with $(NH_4)_2SO_4$ and a series of chromatographies employing Sephadex G-50, Octyl-Sepharose, Q-Sepha- rose, and Biogel P-100. The enzyme was a monomer of 45 kDs as determined through SDS-PAGE and Sephacryl S-200 chromatography. The purified enzyme showed a preference of $\alpha$-D-galactose to $\beta$-D-galactose as a substrate about 5.4 times. Sulfhydryl specific reagents such as N-ethylmaleimide and iodoacetamide significantly inhibited the enzyme activity to the extents of 48 and 52% of its initial activity, respectively. The optimumpH range of $\alpha$-D-galactosidase was around 6.5-7.0. The enzyme activity increased by 46% in the presence of 1mM $Fe^{2+}$.

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Influence of Gibberellic Acid on α-D-Galactosidase Activity in the Grape Berry

  • Kang, Han-Chul;Lee, Seon-Hwa;Kim, Jong-Bum
    • Journal of Applied Biological Chemistry
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    • v.44 no.2
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    • pp.53-58
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    • 2001
  • Glycosidase activities in the grape flesh (Marguerite) were assayed, and the order of activity was marked as follows: ${\alpha}$-D-galactosidase>${\alpha}$-D-mannosidase>${\alpha}$-D-glucosidase>${\beta}$-D-galactosidase>${\beta}$-D-glucosidase. Of these glycosidases, ${\alpha}$- and ${\beta}$-D-galactosidases were prominently expressed by the treatment of gibberellic acid, resulting in 56 and 238% increase of activity, respectively. Most of ${\alpha}$-D-galactosidase was found in the flesh texture, and the activity increase by gibberellic acid occurred mostly in this tissue. The increase in ${\alpha}$-D-galactosidase activity was dependent on the concentration of gibberellic acid treated, showing a positive correlation. Gibberellic acid affected the content of total protein in the grape flesh, 49% increase by 75 ppm treatment. Above this concentration, higher gibberellic acid level did not influence the protein expression. Specific activity of the ${\alpha}$-D-galactosidase still increased, showing 24% increase in activity. Grape flesh subjected by gibberellic acid (100 ppm) resulted in the increased activity against a natural substrate, stachyose, showing 55% increase in activity from the grapes treated with 100 ppm of gibberellic acid. Other natural substrates, such as melibiose and raffinose, were also considerably hydrolyzed, and the extent was similar to that of stachyose hydrolysis. During postharvest storage, ${\alpha}$-D-galactosidase activity in the grape flesh increased by 51% after 20 days and then declined slowly.

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Changes of Glycosidase Activity of Frozen-Thawed Spermatozoa in Human

  • Lee, Chae-Sik;Lee, Sang-Chan;Lee, Ji-Eun;Cheong, Hee-Tae;Yang, Boo-Keun;Park, Choon-Keun
    • Reproductive and Developmental Biology
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    • v.35 no.2
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    • pp.185-190
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    • 2011
  • To evaluate the effect of spermatozoa culture on glycosidase activity of frozen-thawed spermatozoa in human, the spermatozoa were treated experimentally and assayed for activities of ${\alpha}$-L-fucosidase, ${\alpha}$-D-mannosidase, ${\beta}$-D-galactosidase and N-acetyl-${\beta}$-D-glucosaminidase (${\beta}$-GlcNAc'ase). The ${\beta}$-GlcNAc'ase activity was at least two-folds higher than other glycosidases regardless of spermatozoa incubation (p<0.05). The spermatozoa motility was decreased with incubation periods, but no effects by different glycosidases on the changes of spermatozoa motility during the various periods of incubation. In all glycosidases, the spermatozoa-zona binding rates in spermatozoa without incubation were higher than in spermatozoa incubated for 2 h (p<0.05). ${\beta}$-GlcNAc'ase is present mainly in the plasma membrane of spermatozoa frozen-thawed in human. It was also shown that the glycosidase activity was increased in all glycosidases in spite of lower sperm-zona binding by spermatozoa incubation.

Effects of Ginseng Saponin on the Lysosomal Enzyme Activities in Streptozotocin-induced Diabetic Mice (인삼 Saponin이 Lysosome 효소 활성에 미치는 영향)

  • 문창규;김희수;김강석
    • Journal of Food Hygiene and Safety
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    • v.9 no.3
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    • pp.105-109
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    • 1994
  • Lysosomal enzymes might play a most important role in the pathogenesis od diabetic microangiopathy. Some glycosidases, which participate in the catabolism of glycoprotein, are significantly decreased in diabetic mice. In search of new potential lysosomal enzyme inducers, we examined the effects of crude red-ginseng saponin fraction on N-acetyl-$\beta$-D-glucosaminidase, $\beta$-D-galactosidase and $\alpha$-D-mannosidase activities in the liver and kidney of normal and streptozotocin induced diabetic mice. It was found that i.p. administration of ginseng saponin produced the induction of lysosomal enzymes in the kidney more intensively than in the liver. The obtained results suggest the possibility that ginseng saponin might prevent the diabetic microangiopathy.

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The Effect of Fertilization-Promoting Peptide on Fertilizing Ability and Glycosidase Activity In Vitro of Frozen-Thawed Boar Spermatozoa

  • Hwang, I.S.;Park, C.K.;H.T. Cheong;B.K. Yang;Kim, C.I.
    • Proceedings of the KSAR Conference
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    • 2001.03a
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    • pp.43-43
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    • 2001
  • This study evaluated the effect of fertilization-promoting peptide (FPP) on fertilizing ability and glycosidase activity in vitro of spermatozoa frozen-thawed in pig, Using chlortetracycline fluorescence analysis, the various glycosidase analyses and the oocyte penetration test, we have obtained evidence that FPP can promote the fertilizing ability and glycosidase activity of frozen-thawed spermatozoa in vitro. When frozen-thawed spermatozoa was washed with different concentrations of FPP, there were significantly (P<0.05) more acrosome-reacted in medium with 100 nM than 0, 50, 200 and 400 nM. The penetration rates were also highest in medium containing with 100 nM FPP (P<0.05). On the other hand, the $\beta$-N-acetylglucosaminidase activity was at least twofold higher than other glycosidase. In same glycosidase, however, there were no difference in medium with different concentrations of FPP In another experiment, spermatozoa preincubated in medium with or without FPP for 0, 1, 2, 3 and 4 h were inseminated with oocytes matured in vitro. The percentages of spermatozoa that reached acrosome reaction were affected by preincubation and were higher in medium with that than without FPP. When oocytes were inseminated with spermatozoa preincubated in medium with and without FPP during the different periods, however, penetration rates were decreased with preincubation periods of spermatozoa. On the other hand, when the sperm-oocyte were cultured for 4, 8, 12, 16, 20 and 24 h, the penetration rates were higher in spermatozoa preincubated with that than without FPP and had a tendency to increase as time of culture periods. However, The activities of $\alpha$-fucosidase, $\alpha$ -mannosidase, $\beta$-galactosidase and N-acetyl- $\beta$-D-glucosaminidase were higher in medium with that than without FPP regardless of periods of sperm preincubation and sperm-oocyte culture. These results suggest that FPP may play a positive role in promoting of sperm function and glycosidase activity in vitro in pig.

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Effects of Carbohydrase Supplement on Lactation Performance of Primiparous Sows Fed Corn-Soybean Meal Based Lactation Diet

  • Ji, F.;Kim, S.W.
    • Asian-Australasian Journal of Animal Sciences
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    • v.17 no.4
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    • pp.533-537
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    • 2004
  • The experiment was conducted to test the hypothesis that supplementing diets of lactating first parity sows with a mixture of carbohydrases (CS) improves lactation performance and second parity reproductive performance. The CS used in this study contained 7 units/g of $\alpha$-1,6-galactosidase, 22 units/g of $\beta$-1,4-mannanase, $\beta$-1,4-mannosidase and trace amounts of other enzymes. Twenty primiparous sows (Newsham Hybrid) were allotted to either the control group (no CS supplement) or the CS group (0.1% CS supplement) and fed the experimental diets during 21 d lactation period. Sows and nursing pigs were weighed at birth and weekly until weaning. Days of weaning-to-estrus were recorded. Sows had free access to feed and water. Feed intake of sows was measured daily. During the second parity gestation and lactation, all the sows were fed the same gestation and lactation diets and their reproductive performance was measured. During the second parity, there were 14 sows (7 sows per group) remained productive. For the first lactation, maternal body weight loss of the CS group was smaller (p<0.05) than that of the control group. There was no difference in litter weight gain between two groups. Voluntary feed intake of sows did not differ between the two groups. Days of weaning-to-estrus of the CS group were smaller (p<0.05) than those of the control group. In the second parity, there was no difference in the reproductive performance between the two groups. In conclusion, supplementing CS in the diet of lactating sows during the first parity decreased body weight loss and days of weaning-to-estrus of sows. However, these effects of the CS supplementation in the first parity were not successfully carried over to the second parity.