A splice variant of arrestin from human retina
WC SMITH - Experimental eye research, 1996 - Elsevier
Retinal arrestin is known to participate in the quenching of phototransduction through
binding to light-activated and phosphorylated rhodopsin. Recently, a splice variant of retinal
arrestin was identified in bovine photoreceptors which could bind unphosphorylated
photoactive rhodopsin. In this report, a splice variant of retinal arrestin is identified in the
human retina. The variant of human arrestin is produced by splicing out exon 12, unlike the
bovine variant which is produced by splicing out exon 16. This 78bp deletion in the human …
binding to light-activated and phosphorylated rhodopsin. Recently, a splice variant of retinal
arrestin was identified in bovine photoreceptors which could bind unphosphorylated
photoactive rhodopsin. In this report, a splice variant of retinal arrestin is identified in the
human retina. The variant of human arrestin is produced by splicing out exon 12, unlike the
bovine variant which is produced by splicing out exon 16. This 78bp deletion in the human …