Purification and characterization of three MEKA-like proteins in liver: association of a 94 kDa protein with beta gamma subunits of G-proteins.
Retinal 32 kDa MEKA protein (rMEKA) exists in the photoreceptor cells and forms a complex with beta gamma subunit of transducin. Bovine liver contained three MEKA-like proteins (94 kDa, 35 kDa-a, 35 kDa-b) which reacted with a rMEKA antibody. Each protein was purified as a single band on a SDS-PAGE and used for a reconstitution experiment with alpha and beta gamma subunits of cerebral G-proteins (Go/i). The 94 kDa protein inhibited GTP-binding ability of G alpha by forming a complex with beta gamma subunit.
Kuo
C H
CH
Department of Pharmacology, Osaka University Medical School, Japan.
Taira
E
E
Takaha
N
N
Sohma
H
H
Akino
T
T
Fukada
Y
Y
Sanada
K
K
Miki
N
N
D000818:Animals; D002417:Cattle; D005136:Eye Proteins / Q000302:isolation & purification / Q000378:metabolism*; D020555:GTP-Binding Protein Regulators; D019204:GTP-Binding Proteins / Q000378:metabolism*; D006160:Guanosine Triphosphate / Q000378:metabolism; D066298:In Vitro Techniques; D008099:Liver / Q000737:chemistry*; D008970:Molecular Weight; D010750:Phosphoproteins; D015398:Signal Transduction
D005136:Eye Proteins; D020555:GTP-Binding Protein Regulators; D010750:Phosphoproteins; C065631:phosducin; D006160:Guanosine Triphosphate; D019204:GTP-Binding Proteins