Solubilization, physiological role, and localization of a key protein (31.5 kD) to excitation-contraction coupling process of frog skeletal muscle cells, using phenylglyoxal.
A new phenylglyoxal-binding protein (31.5 kD) was solubilized from frog skeletal muscle. The monoclonal AB against the 31.5 kD protein inhibited extracellularly E-C coupling process of single-muscle fibers.
Fujino
S
S
Department of Pharmacology, Hokkaido Institute of Pharmaceutical Sciences, Otaru, Japan.
Fujino
M
M
Satoh
K
K
Nakai
T
T
Kado
T
T
Arima
T
T
Fujino
M
M
D000818:Animals; D000911:Antibodies, Monoclonal; D002110:Caffeine / Q000494:pharmacology; D002352:Carrier Proteins / Q000302:isolation & purification / Q000502:physiology*; D066298:In Vitro Techniques; D008970:Molecular Weight; D009119:Muscle Contraction / Q000187:drug effects / Q000502:physiology*; D009132:Muscles / Q000187:drug effects / Q000502:physiology*; D010658:Phenylglyoxal / Q000494:pharmacology*; D011898:Ranidae
D000911:Antibodies, Monoclonal; D002352:Carrier Proteins; D002110:Caffeine; D010658:Phenylglyoxal