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J. Biol. Chem., Vol. 263, Issue 35, 18688-18692, 12, 1988
JW Crabb, S Goldflam, SE Harris and JC Saari
A 1173-base pair cDNA encoding bovine cellular retinaldehyde-binding
protein (CRALBP) was cloned from a bovine retinal cDNA expression library
using as probes both anti-CRALBP polyclonal and monoclonal antibodies. The
amino acid sequence deduced from the cDNA corresponds exactly to that
determined by direct analysis of NH2-terminally acetylated bovine CRALBP
(Crabb, J. W., Johnson, C. M., Carr, S. A., Armes, L. G., and Saari, J. C.
(1988) J. Biol. Chem. 263, 18678-18687). Nick-translated bovine CRALBP cDNA
probes were then used to clone from a human retinal cDNA library a
1317-base pair cDNA encoding human CRALBP. Bovine and human CRALBP are 92%
identical in amino acid sequence and not related to any other known protein
sequence. Both the bovine and human proteins contain 316 residues and have
calculated molecular weights of 36,378 and 36,347, respectively, exclusive
of the NH2-terminal blocking groups. The CRALBP cDNA clones should prove
valuable as tools for studying the physiological role of the protein in
vision and visual disorders.
Cloning of the cDNAs encoding the cellular retinaldehyde-binding protein from bovine and human retina and comparison of the protein structures
W. Alton Jones Cell Science Center, Inc., Lake Placid, New York 12946.
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