Abstract
Photoreceptor guanylyl cyclase activity is modulated by an endogenous calcium-binding protein called recoverin. A modified isolation procedure for recoverin using gel-filtration chromatography instead of a heat denaturation step is presented. The elution volume of recoverin corresponds to a monomer. Recoverin exhibits a calcium-dependent mobility shift in a native gel electrophoresis. Isoelectric focusing revealed a pI of 5.25. No subspecies of recoverin were detected.
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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Animals
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Antibodies
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Antigens, Neoplasm / analysis
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Antigens, Neoplasm / immunology
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Antigens, Neoplasm / isolation & purification*
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Calcium-Binding Proteins / analysis
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Calcium-Binding Proteins / immunology
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Calcium-Binding Proteins / isolation & purification*
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Cattle
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Chromatography, Gel
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Enzyme Activation
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Eye Proteins*
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Guanylate Cyclase / metabolism*
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Hippocalcin
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Lipoproteins*
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Nerve Tissue Proteins*
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Photoreceptor Cells / metabolism*
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Recoverin
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Rhodopsin / analysis
Substances
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Antibodies
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Antigens, Neoplasm
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Calcium-Binding Proteins
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Eye Proteins
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Lipoproteins
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Nerve Tissue Proteins
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Recoverin
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Hippocalcin
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Rhodopsin
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Guanylate Cyclase