한국막학회:학술대회논문집 (Proceedings of the Membrane Society of Korea Conference)
- 한국막학회 1998년도 춘계 총회 및 학술발표회
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- Pages.31-35
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- 1998
Recognition of substrates by membrane potential
- Yun, Kyu-sik (Department of Natural Fiber Sciences, Seoul National University) ;
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Tak, Tae-moon
(Department of Natural Fiber Sciences, Seoul National University) ;
- Kim, Jong-ho (Department of Textile Engineering, Sang-Ju University)
- 발행 : 1998.04.01
초록
1. INTRODUCTION : Recognition and binding of organic substrates by biological molecules are of vital importance in biophysics and biophysical chemistry. Most studies of the application focused on the development of biosensors, which detected reaction products generated by the binding between enzymes and substrates. Other types of biosensors in which membrane proteins (e.g., nicotinic acetylcholine receptor, auxin receptor ATPase, maltose bining protein, and glutmate receptor) were utilized as a receptor function were also developed. In the previous study[1], the shifts in membrane potential, caused by the injection of substrates into a permeation cell, were measured using immobilized glucose oxidase membranes. It was suggested that the reaction product was not the origin of the potential shifts, but the changes in the charge density in the membrane due to the binding between the enzyme and the substrates generated the potential shifts. In this study, $\gamma$-globulin was immobilized (entrapped) in a poly($\gamma$-amino acid) network, and the shifts in the membrane potential caused by the injection of some amino acids were investigated.
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