The primary structure of iodopsin, a chicken red‐sensitive cone pigment

FEBS Letters

Imamoto, Yasushi¹  Shimura, Yoshiro¹  Yasuda, Kunio¹  Kojima, Daisuke¹  Morodome, Akihiro¹  Kuwata, Osamu¹  Okano, Toshiyuki¹  Yoshizawa, Tôru¹  Shichida, Yoshinori¹  Fukada, Yoshitaka¹  Matsumoto, Hiroki¹  Kokame, Koichi¹ 

[1] Department of Biophysics, Faculty of Science, Kyoto University, Kyoto 606, Japan

关键词: Iodopsin;    Cone visual pigment;    Color vision;    Primary structure;    cDNA cloning;    Chicken retina;   

DOI  :  10.1016/0014-5793(90)80465-U

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A purified iodopsin was digested by CNBr or several proteolytic enzymes into fragments, the amino acid sequences of which were determined. A partial sequence of the C-terminal fragment was utilized for synthesizing an oligonucleotide probe which identified the iodopsin cDNA (1339 bases). The deduced amino acid sequence (362 residues) had 80%, 42% or 43% homology to that of human red-sensitive cone pigment, cattle or chicken rhodospin, respectively. Although the hydropathy profile implies that iodopsin, like rhodopsin, has 7 transmembrane α-helical segments, iodopsin may have a hydrophilic pocket near the seventh segment on the basis of the unexpected cleavages in the middle of the segment VII by chymotrypsin under nondenaturing conditions.

【 授权许可】

Unknown