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Your search keyword '"Jin Sook Cho"' showing total 3 results
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3 results on '"Jin Sook Cho"'

1. Preparation and characterization of alpha-D-glucopyranosyl-alpha-acarviosinyl-D-glucopyranose, a novel inhibitor specific for maltose-producing amylase

Author

Myo-Jeong Kim, Hee-Seob Lee, Jin-Sook Cho, Tae-Jip Kim, Tae-Wha Moon, Sang-Taek Oh, Jung-Wan Kim, Byung-Ha Oh, and Kwan-Hwa Park

Subjects
Biochemistry -- Research, Glucose -- Physiological aspects, Chemical inhibitors -- Physiological aspects, Amylases -- Physiological aspects, Biological sciences, Chemistry
Abstract

Research has been conducted on the maltose-producing amylase inhibitor. The preparation of this inhibitor carried out via the high-molecular-weight acarbose degradation is described.

Published
2002

2. Preparation and Characterization of α-<scp>d</scp>-Glucopyranosyl-α-acarviosinyl-<scp>d</scp>-glucopyranose, a Novel Inhibitor Specific for Maltose-Producing Amylase

Author

Heeseob Lee, Jung-Wan Kim, Tae-Jip Kim, Myo-Jeong Kim, Kwan-Hwa Park, Tae-Wha Moon, Byung-Ha Oh, Sang-Taek Oh, and Jin-Sook Cho

Subjects
Conformational change, Stereochemistry, Dimer, Molecular Sequence Data, Oligosaccharides, Biochemistry, Hydrolysis, chemistry.chemical_compound, medicine, Amylase, Enzyme Inhibitors, Maltose, Chromatography, High Pressure Liquid, Acarbose, chemistry.chemical_classification, biology, Chemistry, Thermus, biology.organism_classification, Enzyme, Carbohydrate Sequence, Amylases, biology.protein, Chromatography, Thin Layer, medicine.drug
Abstract

A novel inhibitor against maltose-producing alpha-amylase was prepared via stepwise degradation of a high-molecular-weight acarbose (HMWA) using Thermus maltogenic amylase (ThMA). The structure of the purified inhibitor was determined to be alpha-D-glucopyranosyl-alpha-acarviosinyl-D-glucopyranose (GlcAcvGlc) by (13)C NMR and MALDI-TOF/MS. Progress curves of PNPG2 hydrolysis by various amylolytic enzymes, including MGase, ThMA, and CDase I-5, in the presence of acarbose or GlcAcvGlc indicated a slow-binding mode of inhibition. Analytical ultracentrifugation and X-ray crystallography analyses revealed that the presence of GlcAcvGlc increased the dimerization of ThMA. The formation of dimer complexed with GlcAcvGlc might induce a conformational change in ThMA, leading to a two-step inhibition process. The inhibition potency of GlcAcvGlc for MGase, ThMA, and CDase I-5 was 3 orders of magnitude higher than that of acarbose. more...

Published
2002
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