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Byung-Gee Kim

Researcher at Seoul National University

Publications -  410
Citations -  10826

Byung-Gee Kim is an academic researcher from Seoul National University. The author has contributed to research in topics: Streptomyces coelicolor & Gene. The author has an hindex of 52, co-authored 382 publications receiving 9479 citations. Previous affiliations of Byung-Gee Kim include New Generation University College & Chungnam National University.

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Microfluidic chip for biochemical reaction and electrophoretic separation by quantitative volume control

TL;DR: In this paper, a microfluidic integrated chip with all the fluidic manipulations required for biochemical reaction and electrophoretic separation was developed, and a novel Y-shaped sample injector was developed as an important interface for the successful combination of the biochemical reaction with electrophic separation.
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Simultaneous profiling of N-glycans and proteins from human serum using a parallel-column system directly coupled to mass spectrometry.

TL;DR: A method for the rapid identification of proteins and their N-glycans was developed through the use of two parallel columns directly connected to a mass spectrometer, suitable for high-throughput analysis and automation, and can be applied to glycomics and proteomics.
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Cell-free Escherichia coli-based system to screen for quorum-sensing molecules interacting with quorum receptor proteins of Streptomyces coelicolor.

TL;DR: A rapid and effective screening tool based on a cell-free Escherichia coli-based expression system to identify QS molecules of Streptomyces and it is shown that N-hexanoyl-dl-homoserine lactone, one of theQS molecules in many gram-negative bacteria, can regulate ScbR and trigger precocious antibiotic production in S. coelicolor.
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Lipase-catalyzed synthesis of lysophosphatidylcholine using organic cosolvent for in situ water activity control

TL;DR: In this article, the role of solvent with regard to changes in substrate solubility, the water activity of the reaction system, and the water content of the enzyme was studied with the aim of finding an operating window for Lysophosphatidylcholines (LPC) production.
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Characterization of GDP-mannose Pyrophosphorylase from Escherichia Coli O157:H7 EDL933 and Its Broad Substrate Specificity

TL;DR: GDP-mannose pyrophosphorylase gene of Escherichia coli O157 was cloned and expressed as a highly soluble protein in E. coli BL21 (DE3) and showed very broad substrate specificities for four nucleotides and various hexose-1-phosphates.