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N‐terminal sequence homology among retinoid‐binding proteins from bovine retina
Author(s) -
Crabb John W.,
Saari John C.
Publication year - 1981
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(81)80655-2
Subject(s) - library science , computer science
Bovine retina contains at least 4 proteins which form relatively stable, one-to-one complexes with retinoids including rhodopsin, the membrane bound visual pigment, and 3 water soluble proteins [l-3]. The characteristics of the latter 3 proteins are quite similar in that each is acidic, 2 are of equal molecular mass and the third has a molecular mass twice the value of the others. These proteins, distinct from the serum retinol-binding protein (SRBP,Mr 21 000) [4], have been termed cellular retinol-binding protein (CRBP, Mr 16 500) [5], cellular retinoic acid-binding protein (CRABP,Mr 16 500) [5] and cellular retinalbinding protein (CRALBP,M, 33 000) [3]. CRABP and CRBP have been purified to apparent homogeneity from several tissues in addition to retina [6-91 whereas CRALBP appears to be a retina-specific protein [lo]. Although serum and cellular retinoid-binding proteins would seem to form a family of structurally related proteins, no evidence for this has appeared. Immunological studies have revealed that antibodies directed toward bovine retinal CRALBP fail to cross-react with bovine retinal CRBP, CRABP, bovine SRBP or bovine opsin [ 111. In addition antibodies against rat SRBP have been shown not to react with rat liver CRBP by two laboratories [8,12] and antibodies directed against rat liver CRBP have been shown not to react with either rat SRBP or rat liver CRABP [ 131. The amino acid sequence of rat liver CRBP was reported not to