Abstract
Rat alanine aminopeptidase was purified from kidney by isolation of the brush border membrane with CaCl2 followed by differential centrifugation and tryptic proteolysis. It is a glycoprotein with a molecular weight of approximately 210,000 daltons comprising two 110,000-dalton subunits and has an amino acid composition similar to that of the human enzyme. Two zinc atoms are covalently bound to each protein subunit.
MeSH terms
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Amino Acids / analysis
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Aminopeptidases / immunology
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Aminopeptidases / isolation & purification*
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Aminopeptidases / metabolism
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Animals
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CD13 Antigens
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Chemical Precipitation
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Chromatography, High Pressure Liquid
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Chromatography, Ion Exchange
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Electrophoresis, Polyacrylamide Gel
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Glycoproteins / isolation & purification
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Immunodiffusion
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Kidney / enzymology*
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Kinetics
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Molecular Weight
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Rats
Substances
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Amino Acids
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Glycoproteins
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Aminopeptidases
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CD13 Antigens