title: Isolation and characterization of rat kidney alanine aminopeptidase.
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.
authors.forename: J L
authors.initials: JL
authors.lastname: Sansot
authors.forename: C
authors.initials: C
authors.lastname: Philippon
authors.forename: A
authors.initials: A
authors.lastname: Colle
authors.forename: D
authors.initials: D
authors.lastname: Prevot
authors.forename: Y
authors.initials: Y
authors.lastname: Manuel
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000626:Aminopeptidases / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism; D000818:Animals; D018826:CD13 Antigens; D011232:Chemical Precipitation; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006023:Glycoproteins / Q000302:isolation & purification; D005779:Immunodiffusion; D007668:Kidney / Q000201:enzymology*; D007700:Kinetics; D008970:Molecular Weight; D051381:Rats
chemical_list: D000596:Amino Acids; D006023:Glycoproteins; D000626:Aminopeptidases; D018826:CD13 Antigens