Abstract
A novel skin-type fatty acid-binding protein, termed cutaneous(C)-FABP, has been purified from rat skin and a cDNA clone for this protein has been identified. The purified protein had the ability to bind long chain fatty acids like other rat FABPs. The deduced amino acid sequence of the cDNA clone comprises residues yielding a molecular mass for the polypeptide of 15.1 kDa and exhibits around 50% identity to myelin P2 protein, adipocyte FABP and heart FABP. Our results propose that C-FABP is a new member of the FABP family.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Adipocytes / metabolism
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Amino Acid Sequence
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Animals
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Base Sequence
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Carrier Proteins / biosynthesis*
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Carrier Proteins / genetics
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Carrier Proteins / isolation & purification
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Cloning, Molecular / methods
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Cytosol / metabolism
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DNA, Complementary / metabolism
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Electrophoresis, Polyacrylamide Gel
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Fatty Acid-Binding Protein 7
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Fatty Acid-Binding Proteins
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Fatty Acids / metabolism
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Gene Library
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Kinetics
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Molecular Sequence Data
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Molecular Weight
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Myocardium / metabolism
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Neoplasm Proteins*
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Nerve Tissue Proteins*
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Organ Specificity
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Rats
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Rats, Sprague-Dawley
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Sequence Homology, Amino Acid
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Skin / metabolism*
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Stearic Acids / metabolism
Substances
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Carrier Proteins
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DNA, Complementary
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Fabp7 protein, rat
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Fatty Acid-Binding Protein 7
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Fatty Acid-Binding Proteins
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Fatty Acids
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Neoplasm Proteins
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Nerve Tissue Proteins
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Stearic Acids
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stearic acid