Leucine aminopeptidase - Open Access .click

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1967
Publisher Summary This chapter describes the mechanism of Leucine Aminopeptidase (LAP). LAP releases amino acids sequentially from the amino terminus of a peptide and the use of the enzyme complements studies with carboxypeptidases. Several large peptides, including glucagon that contains 16 types of amino acid, are cleaved completely by LAP.
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Leucine aminopeptidase from human urine.

Biochemistry international, 1984
L-Leucine aminopeptidase has been partially purified from human urine by DEAE-Sephadex and CM-Sephadex chromatography followed by Sephadex G-150 filtration. The specificity toward various substrates, kinetic properties, metal activation and pH activity are reported.
A, Antonucci, S P, Solinas
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LEUCINE AMINOPEPTIDASE IN THE THYMUS

Cells Tissues Organs, 1962
L K, KORHONEN, S, RUPONEN
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Regarding Leucine Aminopeptidase

New England Journal of Medicine, 1959
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[Leucine aminopeptidase].

Nihon rinsho. Japanese journal of clinical medicine, 1968
Y, Takaoka, C, Hiwaki, M, Takamori
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Leucine Aminopeptidase

2015
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Serum Leucine Aminopeptidase

BMJ, 1960
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Studies on leucine aminopeptidase