Results 141 to 150 of about 3,849 (186)
E K, PATTERSON, S H, HSIAO, A, KEPPEL
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Bioactive Compounds as Modulators of N-Formyl Peptide Signaling in Chronic Diseases. [PDF]
Alvarenga L +5 more
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Proteomic Insight Into the Ontogeny of Blood-Meal Digestion in the Tick Ixodes ricinus. [PDF]
Kozelková T +8 more
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Targeting Glycolysis with 2-Deoxy-D-Glucose and Lysosomal Integrity with L-Leucyl-L-Leucine Methyl Ester as Antimelanoma Strategy. [PDF]
Kosic M +6 more
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Characterization and structural analysis of a leucine aminopeptidase using site-directed mutagenesis. [PDF]
Men Y +6 more
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[SERUM LEUCYL-AMINOPEPTIDASE ACTIVITY IN DISEASES OF THE LIVER, BILE DUCTS AND PANCREAS].
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Characterisation of leucyl aminopeptidase from Solanum tuberosum tuber
Food Chemistry, 2010Abstract 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.
Vujčić, Zoran +5 more
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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, B, Lauffart, A, Gibson
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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, B, Lauffart, A, Gibson
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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 +5 more
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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 +5 more
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Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 2003
Exopeptidases of Morimus funereus larvae were partially purified and characterized. Specific leucyl aminopeptidase (LAP) activity was increased eight-fold by gel filtration of the crude midgut extract. The partially purified LAP had a molecular mass greater than 100 kDa with pH optima from 7.0-9.0 and no strict substrate specificity. M.
Božić, Nataša +3 more
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Exopeptidases of Morimus funereus larvae were partially purified and characterized. Specific leucyl aminopeptidase (LAP) activity was increased eight-fold by gel filtration of the crude midgut extract. The partially purified LAP had a molecular mass greater than 100 kDa with pH optima from 7.0-9.0 and no strict substrate specificity. M.
Božić, Nataša +3 more
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