TY - JOUR
T1 - Recognition of substrates by membrane potential of immobilized glucose oxidase membranes
AU - Higuchi, Akon
AU - Hara, Mariko
AU - Yun, Kyu‐Sik ‐S
AU - Tak, Tae‐Moon ‐M
PY - 1994/3/7
Y1 - 1994/3/7
N2 - The shifts in membrane potential, caused by the injection of glucose into a permeation cell, were measured using immobilized (entrapped) glucose oxidase membranes. No, pH change in the permeation cell was observed upon injection of glucose, but the shift in membrane potential was definitely detected. The shift in membrane potential was observed under nitrogen bubbling (in the absence of oxygen) using initially used enzyme membranes. It was, therefore, suggested that the shifts in membrane potential were not caused by an enzyme‐substrate reaction, but by binding of the substrate to the enzyme, which indues a conformational change in the enzyme and leads to a change in charge density in the enzyme membrane. This mechanism is also supported by the fact that the shifts in membrane potential were observed upon injection of not only D‐glucose but also L‐glucose as reported in our previous study [J. Chem. Soc. Faraday Trans., 87, 695 (1991)]. © 1994 John Wiley & Sons, Inc.
AB - The shifts in membrane potential, caused by the injection of glucose into a permeation cell, were measured using immobilized (entrapped) glucose oxidase membranes. No, pH change in the permeation cell was observed upon injection of glucose, but the shift in membrane potential was definitely detected. The shift in membrane potential was observed under nitrogen bubbling (in the absence of oxygen) using initially used enzyme membranes. It was, therefore, suggested that the shifts in membrane potential were not caused by an enzyme‐substrate reaction, but by binding of the substrate to the enzyme, which indues a conformational change in the enzyme and leads to a change in charge density in the enzyme membrane. This mechanism is also supported by the fact that the shifts in membrane potential were observed upon injection of not only D‐glucose but also L‐glucose as reported in our previous study [J. Chem. Soc. Faraday Trans., 87, 695 (1991)]. © 1994 John Wiley & Sons, Inc.
UR - http://www.scopus.com/inward/record.url?scp=0028767236&partnerID=8YFLogxK
U2 - 10.1002/app.1994.070511006
DO - 10.1002/app.1994.070511006
M3 - 期刊論文
AN - SCOPUS:0028767236
SN - 0021-8995
VL - 51
SP - 1735
EP - 1739
JO - Journal of Applied Polymer Science
JF - Journal of Applied Polymer Science
IS - 10
ER -