TY - JOUR
T1 - Effect of insulin and glucagon on the mobility of ESR-probes incorporated in rat liver plasma membranes
AU - Zlatanov, I.
AU - Maltzeva, E.
AU - Borovok, N.
AU - Spassov, V.
PY - 1993/7
Y1 - 1993/7
N2 - 1. 1. The effect of different concentrations of insulin (INS) and glucagon (GLU) on the rotational mobility of a membrane-incorporated spin probe 2,2-6,6-tetramethyl-4-capriloyl piperidine-1-oxil (C7) was investigated by electron spin resonance (ESR) technique. 2. 2. Two strong adenylate cyclase effectors guanosine 5'-triphosphate (GTP) and guanylyl 5'-imidodiphosphate [Gpp(NH)p], as well as an antioxidant 4-methyl-2,6-ditretbutilphenol (AO) and a nonprotein hormone prostaglandin E2 (PGE2) were used as reference effectors. 3. 3. Applied effectors reduced by 30-82% the rotation correlation time (TR) of the rat liver plasma membranes spin probe C7. The effect was time-dependent and reached saturation 30-40 min after the effector application. 4. 4. The kinetic- and concentration-dependent changes in TR were described by a simple phenomenoloical model. The apparent binding constants and the number of the apparent membrane binding sites of the effectors used were calculated using the model.
AB - 1. 1. The effect of different concentrations of insulin (INS) and glucagon (GLU) on the rotational mobility of a membrane-incorporated spin probe 2,2-6,6-tetramethyl-4-capriloyl piperidine-1-oxil (C7) was investigated by electron spin resonance (ESR) technique. 2. 2. Two strong adenylate cyclase effectors guanosine 5'-triphosphate (GTP) and guanylyl 5'-imidodiphosphate [Gpp(NH)p], as well as an antioxidant 4-methyl-2,6-ditretbutilphenol (AO) and a nonprotein hormone prostaglandin E2 (PGE2) were used as reference effectors. 3. 3. Applied effectors reduced by 30-82% the rotation correlation time (TR) of the rat liver plasma membranes spin probe C7. The effect was time-dependent and reached saturation 30-40 min after the effector application. 4. 4. The kinetic- and concentration-dependent changes in TR were described by a simple phenomenoloical model. The apparent binding constants and the number of the apparent membrane binding sites of the effectors used were calculated using the model.
UR - http://www.scopus.com/inward/record.url?scp=0027285431&partnerID=8YFLogxK
U2 - 10.1016/0020-711X(93)90109-R
DO - 10.1016/0020-711X(93)90109-R
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C2 - 8396052
AN - SCOPUS:0027285431
SN - 0020-711X
VL - 25
SP - 971
EP - 977
JO - International Journal of Biochemistry
JF - International Journal of Biochemistry
IS - 7
ER -