LEUCINE AMINOPEPTIDASE, CYTOSOL FROM HOG KIDNEY, ~100 U/MG

Base Information

• Chemical Name: LEUCINE AMINOPEPTIDASE, CYTOSOL FROM HOG KIDNEY, ~100 U/MG
• CAS No.: 9001-61-0
• Molecular Weight: 0

Synonyms:CorolaseLAP; Cytosol aminopeptidase; Cytosolic aminopeptidase; E.C. 3.4.1.1; E.C.3.4.11.1; FTBL proteins; L-Leucine aminopeptidase; Leucinamide aminopeptidase;Leucinaminopeptidase; Leucine aminopeptidase; Leucine aminopeptidase I; Leucylaminopeptidase; Leucyl peptidase; Proteinates, FTBL; Proteins, FTBL

Chemical Property of LEUCINE AMINOPEPTIDASE, CYTOSOL FROM HOG KIDNEY, ~100 U/MG

Chemical Property:

• Storage Temp.: 2-8°C

Purity/Quality:

98%Min ^*data from raw suppliers

Safty Information:

• Hazard Codes: Xi
• Statements: 36/37/38
• Safety Statements: 26-36

MSDS Files:

Useful:

Refernces

On the activity and specificity of leucine aminopeptidase in eye lenses. Amino acid and dipeptide anilides as substrates.

10.1515/bchm2.1960.322.1.101

The research investigates the activity and specificity of leucine aminopeptidase (LAP) in bovine lenses using amino acid and dipeptide anilides as substrates. The study confirms that bovine lenses contain a significant amount of LAP, which is highly stable and active under optimal conditions (pH 8.5 and 56°C). The enzyme effectively hydrolyzes various amino acid anilides, with leucine anilide showing the highest activity. However, alanine anilide is hydrolyzed by a different enzyme with an optimum pH of 7.5 and temperature of 38°C. The study also demonstrates that the hydrolysis of peptide bonds in dipeptide anilides is significantly higher than that of the amino acid-anilide bond, with leucinamide being hydrolyzed about 30 times faster than its corresponding anilide. Comparative analysis across different species reveals considerable variation in LAP activity, while no significant differences were observed between normal and cataract human lenses.

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