Phosphorylation of interphotoreceptor retinoid-binding protein (IRBP)

Autor:	Ling Lee, C. Lal Kapoor, Barbara Wiggert, Robert L. Somers, Gerald J. Chader
Rok vydání:	1988
Předmět:	Gel electrophoresis Binding protein Cell Biology Interphotoreceptor matrix Biology Molecular biology eye diseases Serine Cellular and Molecular Neuroscience Biochemistry Phosphorylation Tyrosine Threonine Intracellular
Zdroj:	Neurochemistry International. 13:81-87
ISSN:	0197-0186
DOI:	10.1016/0197-0186(88)90106-4
Popis:	The phosphorylation of interphotoreceptor retinoid-binding protein (IRBP), the major soluble (glycolipo) protein of the interphotoreceptor matrix (IPM) and a putative intercellular retinoid-transport vechicle, has been examined in a crude bovine IPM wash using [γ-32P]ATP. SDS-polyacrylamide gel electrophoresis and autoradiography, size-exclusion high-performance liquid chromatography (HPLC) and ion-exchange HPLC all showed IRBP to be phosphorylated in this system. The phosphorylation probably is of serine and/or threonine residues rather than of tyrosine. Interestingly, phosphorylated IRBP was bound tightly to concanvalin A (Con A)-Sepharose and was not eluted by 50 mM α-methyl- d -mannoside indicating a marked alteration in binding characteristics upon phosphorylation.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a4bed04d217612631634ca7b4932999 https://doi.org/10.1016/0197-0186(88)90106-4 Zobrazit plný text záznamu