Abstract:
:cDNA clones encoding a glutamic acid-rich protein were isolated from a bovine retina cDNA expression library. The cDNA sequence contained an open reading frame of 1770 base pairs encoding a protein of 590 amino acids (64,509 Da) and untranslated regions of 60 and 490 base pairs at the 5' and 3' ends, respectively. The cDNA hybridized to a 2.4-kilobase retinal mRNA. The amino acid sequence derived from the cDNA sequence contains a glutamic acid-rich domain in which 68 of 109 amino acids are glutamic acid. In addition, this domain contains four repeats of a peptide of 11 amino acids and two repeats of a peptide of 26 amino acids. A polyclonal antibody raised against a decapeptide corresponding to the undecapeptide repeat sequence reacted with a protein in an extract of bovine rod outer segments, whose molecular mass, 65 kDa, corresponded to that of the above glutamic acid-rich protein. The retinal glutamic acid-rich protein showed homology with glutamic acid-rich proteins from bovine brain and the C-terminal region of mammalian neurofilaments.
journal_name
Proc Natl Acad Sci U S Aauthors
Sugimoto Y,Yatsunami K,Tsujimoto M,Khorana HG,Ichikawa Adoi
10.1073/pnas.88.8.3116subject
Has Abstractpub_date
1991-04-15 00:00:00pages
3116-9issue
8eissn
0027-8424issn
1091-6490journal_volume
88pub_type
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