Identification of a retina-specific MEKA protein as a 33 K protein.
A photoreceptor-specific MEKA protein was purified from bovine retinal soluble fraction. The purified sample was eluted as a single peak of 74 kDa protein from a Superose column, which was dissolved into three components, MEKA protein (32 kDa), beta-(36 kDa) and gamma-(10 kDa) subunits of transducin on a SDS-PAGE. From several lines of evidence, we concluded that MEKA protein is identical with a 33k phosphoprotein reported by Lee et al (1).
Kuo
C H
CH
Department of Pharmacology, Kanazawa University, Japan.
Taniura
H
H
Watanabe
Y
Y
Fukada
Y
Y
Yoshizawa
T
T
Miki
N
N
D000818:Animals; D002417:Cattle; D005136:Eye Proteins / Q000302:isolation & purification* / Q000378:metabolism; D020555:GTP-Binding Protein Regulators; D006863:Hydrogen-Ion Concentration; D046911:Macromolecular Substances; D008970:Molecular Weight; D010750:Phosphoproteins; D012160:Retina / Q000032:analysis; D012995:Solubility; D015293:Transducin / Q000378:metabolism*
D005136:Eye Proteins; D020555:GTP-Binding Protein Regulators; D046911:Macromolecular Substances; D010750:Phosphoproteins; C065631:phosducin; D015293:Transducin