Primary and Secondary Structure of Bovine Retinal S Antigen (48-kDa Protein)

The complete amino acid sequence of bovine S antigen (48-kDa protein) has been determined by cDNA and partial amino acid sequencing. A 1623-base-pair (bp) cDNA contains an open reading frame coding for a protein of 404 amino acids (45,275 Da). Tryptic peptides and cyanogen bromide peptides of native...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1987-10, Vol.84 (20), p.6975-6979
Main Authors: Shinohara, T., Dietzschold, B., Craft, C. M., Wistow, G., Early, J. J., Donoso, L. A., Horwitz, J., Tao, R.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Antigens
Arrestin
Base Sequence
Biochemistry
Biological and medical sciences
Cell physiology
Chemical bases
Circular Dichroism
Complementary DNA
DNA
DNA - genetics
Eye Proteins
Eyes
Fundamental and applied biological sciences. Psychology
genes
Glycoproteins
Libraries
Molecular and cellular biology
Molecular Sequence Data
nucleotide sequence
Open reading frames
Protein Conformation
Proteins
retina
Retina - immunology
S antigen
Sequence Homology, Nucleic Acid
Ungulates
Vision, photoreception
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Summary:The complete amino acid sequence of bovine S antigen (48-kDa protein) has been determined by cDNA and partial amino acid sequencing. A 1623-base-pair (bp) cDNA contains an open reading frame coding for a protein of 404 amino acids (45,275 Da). Tryptic peptides and cyanogen bromide peptides of native bovine S antigen were purified and partially sequenced. All of these peptides were accounted for in the long open reading frame. Searching of the National Biomedical Research Foundation data bank revealed no extensive sequence homology between S antigen and other proteins. However, there are local regions of sequence similarity with α transducin, including the sites subject to ADP-ribosylation by Bordetella pertussis and cholera toxins and the phosphoryl binding-sites. Secondary structure prediction and circular dichroic spectroscopy show that S antigen is composed predominantly of β -sheet conformation. Acid-catalyzed methanolysis suggests the presence of low levels of carbohydrate in the molecule.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.84.20.6975