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Koreyoshi Imamura

Researcher at Okayama University

Publications -  126
Citations -  3325

Koreyoshi Imamura is an academic researcher from Okayama University. The author has contributed to research in topics: Adsorption & Amorphous solid. The author has an hindex of 29, co-authored 122 publications receiving 3044 citations. Previous affiliations of Koreyoshi Imamura include Kyoto University.

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On the adsorption of proteins on solid surfaces, a common but very complicated phenomenon

TL;DR: In this article, the authors stress the importance and interesting aspect of protein adsorption on solid surfaces by reviewing findings that have been obtained in recent years, and stress that information on the conformation of the adsorbed protein as well as adsorbing characteristics is essential for a system's performance.
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Recent Advances in Controlled Immobilization of Proteins onto the Surface of the Solid Substrate and Its Possible Application to Proteomics

TL;DR: This review focuses on recent advances in immobilization methodol- ogy for proteins/enzymes on a surface, including those using the affinity peptides screened by random peptide library sys- tems.
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Adsorption behavior of methylene blue and its congeners on a stainless steel surface.

TL;DR: It was found that the kind of substituent groups at most positions of the polyheterocycles of methylene blue strongly affects the adsorption behavior, particularly the area occupied by an adsorbed dye molecule, the affinity for the stainless steel surface, and the orientation of the adsorsed dye molecule on the Stainless steel surface.
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Effects of Types of Sugar on the Stabilization of Protein in the Dried State

TL;DR: The rehumidification of protein that was freeze-dried in the presence of sugar induced the refolding of protein structure, whereas the protein dried alone did not show any recovery of its native structure.
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Adsorption characteristics of various proteins to a titanium surface.

TL;DR: P pH values that gave maximal sums of irreversibly and reversibly adsorbed proteins were in the pH range of 3-8 and tended to increase slightly with the pI value of the corresponding protein, which was nearly independent of pI.