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C. S. Park - One of the best experts on this subject based on the ideXlab platform.
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Lactose-egg yolk diluent supplemented with N-Acetyl-D-Glucosamine affect acrosome morphology and motility of frozen-thawed boar sperm.
Animal Reproduction Science, 2002Co-Authors: Yoon-sun Yi, Gi-sun Im, C. S. ParkAbstract:Abstract These experiments were carried out to investigate the effect of N -acetyl- d -glucosamine, and to obtain additional information about the effect of orvus es paste (OEP) and egg yolk concentration in the freezing of boar sperm in the maxi-straw. The highest post-thaw acrosomes of normal apical ridge (NAR) and motility were obtained with 0.025 or 0.05% N -acetyl- d -glucosamine concentration in the first diluent. However, there were no effects of N -acetyl- d -glucosamine among the diluents with or without N -acetyl- d -glucosamine at the second dilution. The N -acetyl- d -glucosamine in the first and second diluents was added at room temperatures (20–23 °C) and 5 °C, respectively. It is suggested that the temperature of N -acetyl- d -glucosamine addition is important for the effect of boar sperm protection during freezing and thawing. When the 0.05% N -acetyl- d -glucosamine was supplemented in the first diluent, the optimum final OEP content was 0.5%. The optimum content of egg yolk in the diluent with 0.05% N -acetyl- d -glucosamine concentration was 20% and egg yolk was one of the main cryoprotective agents. In conclusion, we found out that the diluent with 0.025 or 0.05% soluble N -acetyl- d -glucosamine in the first diluent, 0.5% final orvus es paste concentration and 20% egg yolk concentration significantly enhanced NAR acrosomes and motility of boar sperm after freezing and thawing.
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Lactose-egg yolk diluent supplemented with N-Acetyl-D-Glucosamine affect acrosome morphology and motility of frozen-thawed boar sperm.
Animal reproduction science, 2002Co-Authors: Y J Yi, Gi-sun Im, C. S. ParkAbstract:These experiments were carried out to investigate the effect of N-Acetyl-D-Glucosamine, and to obtain additional information about the effect of orvus es paste (OEP) and egg yolk concentration in the freezing of boar sperm in the maxi-straw. The highest post-thaw acrosomes of normal apical ridge (NAR) and motility were obtained with 0.025 or 0.05% N-Acetyl-D-Glucosamine concentration in the first diluent. However, there were no effects of N-Acetyl-D-Glucosamine among the diluents with or without N-Acetyl-D-Glucosamine at the second dilution. The N-Acetyl-D-Glucosamine in the first and second diluents was added at room temperatures (20-23 degrees C) and 5 degrees C, respectively. It is suggested that the temperature of N-Acetyl-D-Glucosamine addition is important for the effect of boar sperm protection during freezing and thawing. When the 0.05% N-Acetyl-D-Glucosamine was supplemented in the first diluent, the optimum final OEP content was 0.5%. The optimum content of egg yolk in the diluent with 0.05% N-Acetyl-D-Glucosamine concentration was 20% and egg yolk was one of the main cryoprotective agents. In conclusion, we found out that the diluent with 0.025 or 0.05% soluble N-Acetyl-D-Glucosamine in the first diluent, 0.5% final orvus es paste concentration and 20% egg yolk concentration significantly enhanced NAR acrosomes and motility of boar sperm after freezing and thawing.
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Effect of N-Acetyl-D-Glucosamine, and glycerol concentration and equilibration time on acrosome morphology and motility of frozen-thawed boar sperm.
Animal reproduction science, 2002Co-Authors: Y J Yi, Y M Cheon, C. S. ParkAbstract:A series of experiments were conducted to determine the effect of N-Acetyl-D-Glucosamine, glycerol concentration and equilibration time for the freezing of boar spermatozoa in 5 ml maxi-straws. The optimum final glycerol concentration in the diluent with 0.05% N-Acetyl-D-Glucosamine in the first diluent was 2-3% and the optimum glycerol equilibration time was 2-3h. In conclusion, we recommend the first diluent containing 11% lactose hydrate, 20% egg yolk and 0.05% N-Acetyl-D-Glucosamine in 100ml distilled water, and the second diluent containing 11% lactose hydrate, 20% egg yolk, 4% glycerol and 1% orvus es paste for the diluents of boar sperm freezing. Also, we found out that 0.05% soluble N-Acetyl-D-Glucosamine was the optimum concentration in the first diluent and a concentration of 0.05% soluble N-Acetyl-D-Glucosamine significantly enhanced the cryopreservation of boar spermatozoa.
A. Datta - One of the best experts on this subject based on the ideXlab platform.
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N-Acetyl-D-Glucosamine specific hemagglutinin receptor of Vibrio cholerae O1 in chicken erythrocyte membranes.
Fems Immunology and Medical Microbiology, 2002Co-Authors: D. Sasmal, B. Guhathakurta, S. K. Bhattacharya, A. DattaAbstract:Abstract N-Acetyl- D -glucosamine specific cell-associated hemagglutinin (HA)/lectin, previously purified from a strain of Vibrio cholerae O1, had been established as an adhesin molecule of V. cholerae O1 cells. This communication records the isolation and purification of the glycoprotein receptor of the N-acetyl- D -glucosamine specific HA of the V. cholerae O1 strain from chicken erythrocyte membranes. The most salient feature of this study is that the pretreatment of partially purified glycoprotein with purified HA could completely inhibit the hemagglutinating activity of the V. cholerae O1 strain with chicken erythrocytes.
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N-Acetyl-D-Glucosamine-specific lectin purified from Vibrio cholerae 01.
Fems Microbiology Letters, 1992Co-Authors: D. Sasmal, B. Guhathakurta, A.n. Ghosh, A. DattaAbstract:Abstract An N- acetyl- D -glucosamine-specific cell associated hemagglutinin (HA) was isolated and purified from a strain of Vibrio cholerae 01 by chitin affinity chromatography followed by separation on Bio Gel P-150. A single stained protein band of 47 kDa in sodium dodecyl sulfate-polyacryl-amide gel electrophoresis (SDS-PAGE) was observed with the purified HA. HA-antisera produced a single precipitin band against the purified HA in an immunodiffusion test without exhibiting any reactivity towards purified lipopolysaccharide (LPS). Purified HA, used as solid-phase antigen in an enzyme-linked immunosorbent assay (ELISA), reacted strongly with HA-antisera but cross-reacted negligibly with antisera raised against purified LPS. Hemagglutinating activity of the purified HA was highly sensitive to N- acetyl- D -glucosamine . The immunogold-labelling method using HA-antisera confirmed the location of the HA on the surface of the bacterial cells. The HA-antisera reacted with
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N-Acetyl-D-Glucosamine-specific lectin purified from Vibrio cholerae 01.
FEMS microbiology letters, 1992Co-Authors: D. Sasmal, B. Guhathakurta, A.n. Ghosh, A. DattaAbstract:An N-Acetyl-D-Glucosamine-specific cell associated hemagglutinin (HA) was isolated and purified from a strain of Vibrio cholerae 01 by chitin affinity chromatography followed by separation on Bio Gel P-150. A single stained protein band of 47 kDa in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was observed with the purified HA. HA-antisera produced a single precipitin band against the purified HA in an immunodiffusion test without exhibiting any reactivity towards purified lipopolysaccharide (LPS). Purified HA, used as solid-phase antigen in an enzyme-linked immunosorbent assay (ELISA), reacted strongly with HA-antisera but cross-reacted negligibly with antisera raised against purified LPS. Hemagglutinating activity of the purified HA was highly sensitive to N-Acetyl-D-Glucosamine. The immunogold-labelling method using HA-antisera confirmed the location of the HA on the surface of the bacterial cells. The HA-antisera reacted with a protein component of the homologous outer membrane preparation. A significant inhibition was observed in the adhesive capability of the V. cholerae 01 strain to isolated rabbit intestinal epithelial cells (RIEC) in vitro when the later were pre-treated with the purified HA.
Y J Yi - One of the best experts on this subject based on the ideXlab platform.
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Lactose-egg yolk diluent supplemented with N-Acetyl-D-Glucosamine affect acrosome morphology and motility of frozen-thawed boar sperm.
Animal reproduction science, 2002Co-Authors: Y J Yi, Gi-sun Im, C. S. ParkAbstract:These experiments were carried out to investigate the effect of N-Acetyl-D-Glucosamine, and to obtain additional information about the effect of orvus es paste (OEP) and egg yolk concentration in the freezing of boar sperm in the maxi-straw. The highest post-thaw acrosomes of normal apical ridge (NAR) and motility were obtained with 0.025 or 0.05% N-Acetyl-D-Glucosamine concentration in the first diluent. However, there were no effects of N-Acetyl-D-Glucosamine among the diluents with or without N-Acetyl-D-Glucosamine at the second dilution. The N-Acetyl-D-Glucosamine in the first and second diluents was added at room temperatures (20-23 degrees C) and 5 degrees C, respectively. It is suggested that the temperature of N-Acetyl-D-Glucosamine addition is important for the effect of boar sperm protection during freezing and thawing. When the 0.05% N-Acetyl-D-Glucosamine was supplemented in the first diluent, the optimum final OEP content was 0.5%. The optimum content of egg yolk in the diluent with 0.05% N-Acetyl-D-Glucosamine concentration was 20% and egg yolk was one of the main cryoprotective agents. In conclusion, we found out that the diluent with 0.025 or 0.05% soluble N-Acetyl-D-Glucosamine in the first diluent, 0.5% final orvus es paste concentration and 20% egg yolk concentration significantly enhanced NAR acrosomes and motility of boar sperm after freezing and thawing.
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Effect of N-Acetyl-D-Glucosamine, and glycerol concentration and equilibration time on acrosome morphology and motility of frozen-thawed boar sperm.
Animal reproduction science, 2002Co-Authors: Y J Yi, Y M Cheon, C. S. ParkAbstract:A series of experiments were conducted to determine the effect of N-Acetyl-D-Glucosamine, glycerol concentration and equilibration time for the freezing of boar spermatozoa in 5 ml maxi-straws. The optimum final glycerol concentration in the diluent with 0.05% N-Acetyl-D-Glucosamine in the first diluent was 2-3% and the optimum glycerol equilibration time was 2-3h. In conclusion, we recommend the first diluent containing 11% lactose hydrate, 20% egg yolk and 0.05% N-Acetyl-D-Glucosamine in 100ml distilled water, and the second diluent containing 11% lactose hydrate, 20% egg yolk, 4% glycerol and 1% orvus es paste for the diluents of boar sperm freezing. Also, we found out that 0.05% soluble N-Acetyl-D-Glucosamine was the optimum concentration in the first diluent and a concentration of 0.05% soluble N-Acetyl-D-Glucosamine significantly enhanced the cryopreservation of boar spermatozoa.
D. Sasmal - One of the best experts on this subject based on the ideXlab platform.
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N-Acetyl-D-Glucosamine specific hemagglutinin receptor of Vibrio cholerae O1 in chicken erythrocyte membranes.
Fems Immunology and Medical Microbiology, 2002Co-Authors: D. Sasmal, B. Guhathakurta, S. K. Bhattacharya, A. DattaAbstract:Abstract N-Acetyl- D -glucosamine specific cell-associated hemagglutinin (HA)/lectin, previously purified from a strain of Vibrio cholerae O1, had been established as an adhesin molecule of V. cholerae O1 cells. This communication records the isolation and purification of the glycoprotein receptor of the N-acetyl- D -glucosamine specific HA of the V. cholerae O1 strain from chicken erythrocyte membranes. The most salient feature of this study is that the pretreatment of partially purified glycoprotein with purified HA could completely inhibit the hemagglutinating activity of the V. cholerae O1 strain with chicken erythrocytes.
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N-Acetyl-D-Glucosamine-specific lectin purified from Vibrio cholerae 01.
Fems Microbiology Letters, 1992Co-Authors: D. Sasmal, B. Guhathakurta, A.n. Ghosh, A. DattaAbstract:Abstract An N- acetyl- D -glucosamine-specific cell associated hemagglutinin (HA) was isolated and purified from a strain of Vibrio cholerae 01 by chitin affinity chromatography followed by separation on Bio Gel P-150. A single stained protein band of 47 kDa in sodium dodecyl sulfate-polyacryl-amide gel electrophoresis (SDS-PAGE) was observed with the purified HA. HA-antisera produced a single precipitin band against the purified HA in an immunodiffusion test without exhibiting any reactivity towards purified lipopolysaccharide (LPS). Purified HA, used as solid-phase antigen in an enzyme-linked immunosorbent assay (ELISA), reacted strongly with HA-antisera but cross-reacted negligibly with antisera raised against purified LPS. Hemagglutinating activity of the purified HA was highly sensitive to N- acetyl- D -glucosamine . The immunogold-labelling method using HA-antisera confirmed the location of the HA on the surface of the bacterial cells. The HA-antisera reacted with
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N-Acetyl-D-Glucosamine-specific lectin purified from Vibrio cholerae 01.
FEMS microbiology letters, 1992Co-Authors: D. Sasmal, B. Guhathakurta, A.n. Ghosh, A. DattaAbstract:An N-Acetyl-D-Glucosamine-specific cell associated hemagglutinin (HA) was isolated and purified from a strain of Vibrio cholerae 01 by chitin affinity chromatography followed by separation on Bio Gel P-150. A single stained protein band of 47 kDa in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was observed with the purified HA. HA-antisera produced a single precipitin band against the purified HA in an immunodiffusion test without exhibiting any reactivity towards purified lipopolysaccharide (LPS). Purified HA, used as solid-phase antigen in an enzyme-linked immunosorbent assay (ELISA), reacted strongly with HA-antisera but cross-reacted negligibly with antisera raised against purified LPS. Hemagglutinating activity of the purified HA was highly sensitive to N-Acetyl-D-Glucosamine. The immunogold-labelling method using HA-antisera confirmed the location of the HA on the surface of the bacterial cells. The HA-antisera reacted with a protein component of the homologous outer membrane preparation. A significant inhibition was observed in the adhesive capability of the V. cholerae 01 strain to isolated rabbit intestinal epithelial cells (RIEC) in vitro when the later were pre-treated with the purified HA.
Kazuya Yamamoto - One of the best experts on this subject based on the ideXlab platform.
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synthesis of chitin and chitosan stereoisomers by thermostable α glucan phosphorylase catalyzed enzymatic polymerization of α d glucosamine 1 phosphate
Organic and Biomolecular Chemistry, 2015Co-Authors: Jun-ichi Kadokawa, Riko Shimohigoshi, Kento Yamashita, Kazuya YamamotoAbstract:The relationship between two aminopolysaccharide stereoisomers, namely α-(1→4)- and β-(1→4)-linked (N-acetyl)-D-glucosamine polymers, is of significant interest within the field of polysaccharide science, as they correspond to amino analogs of the representative abundant natural polysaccharides, viz. amylose and cellulose. While the latter glucosamine polymer is the basis of well-known natural polysaccharides, chitin and chitosan (linear polysaccharides composed of β-(1→4)-linked N-Acetyl-D-Glucosamine and D-glucosamine), to the best of our knowledge, the former (α-(1→4)-linked) has not been observed in nature. For the purpose of these studies, the synthesis of such non-natural aminopolysaccharides was performed by the thermostable α-glucan phosphorylase (from Aquifex aeolicus VF5)-catalyzed enzymatic polymerization of α-D-glucosamine 1-phosphate (GlcN-1-P), via successive α-glucosaminylations, in ammonia buffer containing Mg2+ ions, resulting in the production of the α-(1→4)-linked D-glucosamine polymers, corresponding to the structure of the chitosan stereoisomer. Subsequent N-acetylation of the products gave the aminopolysaccharides, corresponding to the chitin stereoisomer.
