Abstract
A simple immunoaffinity column chromatographic procedure is described whereby recombinant human prorenin secreted from Chinese hamster ovary cells may be isolated in a high state of purity from serum-free culture medium. Prorenin thus purified has been characterized by SDS-polyacrylamide gel electrophoresis and by partial sequence analysis which has revealed the expected N-terminal sequence. Trypsin treatment gives rise to renin, and reversible acid activation has also been demonstrated for the recombinant zymogen.
MeSH terms
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Ammonium Sulfate
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Animals
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Cell Line
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Chemical Precipitation
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Chromatography, Affinity
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Cricetinae
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Cricetulus
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Enzyme Activation
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Enzyme Precursors / biosynthesis
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Enzyme Precursors / isolation & purification*
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Enzyme Precursors / metabolism
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Female
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Humans
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Hydrogen-Ion Concentration
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Immunoassay
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Molecular Weight
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Ovary / metabolism*
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / isolation & purification*
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Recombinant Proteins / metabolism
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Renin / biosynthesis
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Renin / isolation & purification*
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Renin / metabolism
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Trypsin
Substances
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Enzyme Precursors
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Recombinant Proteins
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Trypsin
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Renin
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Ammonium Sulfate