Leucine aminopeptidase from human urine
Biochemistry International
|May 1, 1983
Summary
Human urine L-Leucine aminopeptidase was purified using chromatography and filtration. Its substrate specificity, kinetics, metal activation, and pH activity were characterized.
Area of Science:
- Biochemistry
- Enzymology
Background:
- L-Leucine aminopeptidase is an enzyme found in various biological sources.
- Understanding its properties is crucial for biochemical research.
Purpose of the Study:
- To partially purify L-Leucine aminopeptidase from human urine.
- To characterize its enzymatic properties, including substrate specificity, kinetics, metal activation, and pH dependence.
Main Methods:
- Ion-exchange chromatography using DEAE-Sephadex and CM-Sephadex.
- Gel filtration using Sephadex G-150.
Main Results:
- Partial purification of L-Leucine aminopeptidase was achieved.
- The enzyme's specificity towards different substrates was determined.
- Kinetic parameters, metal ion activation effects, and optimal pH were reported.
Conclusions:
- The study successfully purified and characterized human urinary L-Leucine aminopeptidase.
- The reported properties provide valuable data for understanding leucine aminopeptidase function and regulation.
