| Literature DB >> 2764917 |
C H Kuo1, H Taniura, Y Watanabe, Y Fukada, T Yoshizawa, N Miki.
Abstract
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).Entities:
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Year: 1989 PMID: 2764917 DOI: 10.1016/0006-291x(89)90781-x
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575