Purification and characterization of leucine-specific aminopeptidase from the soluble fraction of human placenta.
A soluble aminopeptidase distinct from two enzymes described previously was isolated from human placenta and some of its properties were investigated. The three aminopeptidases were separated by DEAE-cellulose chromatography. The newly found aminopeptidase exhibits specific hydrolysis of leucine derivatives among various synthetic substrates. However, a broad substrate specificity was observed toward some natural bioactive peptides.
Department of Clinical Biochemistry, Hokkaido Institute of Pharmaceutical Sciences, Japan.
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Y
Kumagai
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Watanabe
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Fujimoto
D000595:Amino Acid Sequence; D002848:Chromatography, DEAE-Cellulose; D005260:Female; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007931:Leucyl Aminopeptidase / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy; D012995:Solubility; D013379:Substrate Specificity
D009842:Oligopeptides; D007931:Leucyl Aminopeptidase