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[SERUM LEUCYL-AMINOPEPTIDASE ACTIVITY IN DISEASES OF THE LIVER, BILE DUCTS AND PANCREAS].

Przeglad epidemiologiczny, 1996
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Purification and characterization of leucyl aminopeptidase and pyroglutamyl aminopeptidase from human s̀keletal muscle

Clinica Chimica Acta, 1991
The purification and characterization of leucyl aminopeptidase and pyroglutamyl aminopeptidase from human skeletal muscle are described. The characteristics of leucyl aminopeptidase were as follows: optimum activity was at pH 9.5 in the presence of 5 mmol/l Mg2+ or 0.5 mmol Mn2+. No activation of enzyme activity was obtained following addition of other
D Mantle, David Mantle, B Lauffart
exaly   +3 more sources

Characterisation of leucyl aminopeptidase from Solanum tuberosum tuber

Food Chemistry, 2010
Abstract Potato juice (a waste product from the starch industry) is a potential source of novel enzymes for food applications. For use in the production and improvement of food protein hydrolysates, commercially available exopeptidases, predominantly aminopeptidases, are recommended.
MIROSLAVA Vujčić, Nataša Bozic, Biljana Dojnov   +2 more
exaly   +4 more sources

A New Member of the Leucyl Aminopeptidase Family Purified and Identified from a Marine Unicellular Algae

Biochemical and Biophysical Research Communications, 1999
Leucyl aminopeptidase (LAP; EC 3.4.11.1) activity was purified from crude extracts of the marine unicellular algae Gonyaulax polyedra by a combination of hydrophobic interaction with phenyl sepharose, DEAE-cellulose, and mono-Q HR5/5 ion-exchange chromatography.
Pio Colepicolo
exaly   +3 more sources

Leucyl aminopeptidase (Fasciola-type)

Neil D Rawlings
exaly   +2 more sources

Structural and immunological evidence for the identity of prolyl aminopeptidase with leucyl aminopeptidase

Biochemical and Biophysical Research Communications, 1991
Prolyl aminopeptidase (EC 3.4.11.5) has been assumed to be a unique enzyme catalyzing specifically the removal of unsubstituted NH2-terminal L-prolyl residues from various peptides and to be distinct from leucyl aminopeptidase (EC 3.4.11.1). In the present study, prolyl aminopeptidases were purified to apparent homogeneity from pig small intestine ...
M, Matsushima, T, Takahashi, M, Ichinose, K, Miki, K, Kurokawa, K, Takahashi   +5 more
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The leucyl aminopeptidase from Helicobacter pylori is an allosteric enzyme

Microbiology, 2005
This study describes the cloning, genetic analysis and biochemical characterization of a leucyl aminopeptidase (LAP) fromHelicobacter pylori. A gene encoding LAP was cloned fromH. pyloriand the expressed 55 kDa protein displayed homology to aminopeptidases from Gram-negative bacteria, plants and mammals.
Lei, Dong, Ni, Cheng, Ming-Wei, Wang, Junfeng, Zhang, Chang, Shu, De-Xu, Zhu   +5 more
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Leucyl/Cystinyl Aminopeptidase Gene Variants in Septic Shock

Chest, 2011
Vasopressin is an essential peptide hormone regulating cardiovascular homeostasis and an adjunctive vasopressor therapy for septic shock.We tested for association between single nucleotide polymorphisms (SNPs) in vasopressin pathway genes and altered outcome in derivation (n = 589) and replication (n = 616) cohorts of patients with septic shock.
Taka-Aki, Nakada, James A, Russell, Hugh, Wellman, John H, Boyd, Emiri, Nakada, Katherine R, Thain, Simone A, Thair, Hiroyuki, Hirasawa, Shigeto, Oda, Keith R, Walley   +9 more
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Biophysical characterization of a recombinant leucyl aminopeptidase from Bacillus kaustophilus

Biochemistry (Moscow), 2010
The biophysical properties of Bacillus kaustophilus leucyl aminopeptidase (BkLAP) were examined in terms of analytical ultracentrifugation, fluorescence spectroscopy, and circular dichroism. By using the analytical ultracentrifuge, we demonstrated that tetrameric BkLAP exists as the major form in solution at protein concentration of 1.5 mg/ml at pH 8.0.
Meng-Chun, Chi, Hui-Ping, Chang, Gu-Gang, Chang, Tzu-Fan, Wang, Hsien-Bin, Huang, Long-Liu, Lin   +5 more
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Screening and In Vitro Evaluation of Potential Plasmodium falciparum Leucyl Aminopeptidase Inhibitors

Current Computer Aided-Drug Design, 2016
Plasmodium falciparum leucyl aminopeptidase (PfA-M17) regulates the intracellular pool of amino acids required for the growth and development of parasites. Thus, PfA-M17 is a promising target for anti-malarial drug development.In the present study, structure-based drug design was used to identify novel PfA-M17 inhibitors, which were subsequently ...
Meenakshi, Chaudhary, Vineeta, Singh, Anup R, Anvikar, Shakti, Sahi   +3 more
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