Phosphorylation of interphotoreceptor retinoid-binding protein (IRBP) |
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| Affiliation: | 1. School of Energy and Power, Jiangsu University of Science and Technology, Zhenjiang 212003, People''s Republic of China;2. Nanjing Ceprei Industrial Technology Research Institute Co., Ltd, Nanjing 211800, People''s Republic of China;3. Institute of Mechanics and Power Engineering, Ogarev Mordovia State University, Saransk 430005, Russia;1. Laboratório de Toxinologia, Instituto Oswaldo Cruz, Fundação Oswaldo Cruz, Rio de Janeiro, Brazil;2. Laboratório de Biologia Celular, Instituto Oswaldo Cruz, Fundação Oswaldo Cruz, Rio de Janeiro, Brazil;3. Laboratório de Proteômica e Engenharia de Proteínas, Instituto Carlos Chagas, Fiocruz, Paraná, Brazil |
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| Abstract: | 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. |
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