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[SERUM LEUCYL-AMINOPEPTIDASE ACTIVITY IN DISEASES OF THE LIVER, BILE DUCTS AND PANCREAS].
Przeglad epidemiologiczny, 1996 openaire +1 more source
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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
David Mantle +2 more
exaly +3 more sources
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
David Mantle +2 more
exaly +3 more sources
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.
Zoran Vujčić +2 more
exaly +4 more sources
Comparative Biochemistry and Physiology - 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.
Nataša Bozic +2 more
exaly +5 more sources
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.
Nataša Bozic +2 more
exaly +5 more sources
Meat Science, 2006
Sixty experimental Jinhua hams were processed by a traditional method. The potential arginyl (RAP) and leucyl (LAP) aminopeptidase activities in biceps femoris were determined. The effects of temperature, salt content, sodium nitrate content and pH value on muscle RAP and LAP activities were evaluated using response surface methodology.
G H Zhou, X L Xu
exaly +3 more sources
Sixty experimental Jinhua hams were processed by a traditional method. The potential arginyl (RAP) and leucyl (LAP) aminopeptidase activities in biceps femoris were determined. The effects of temperature, salt content, sodium nitrate content and pH value on muscle RAP and LAP activities were evaluated using response surface methodology.
G H Zhou, X L Xu
exaly +3 more sources
Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology, 2008
The major leucyl aminopeptidase (LAP) from the midgut of Morimus funereus larvae was purified and characterised. Specific LAP activity was increased 292-fold by purification of the crude midgut extract. The purified enzyme had a pH optimum of 7.5 (optimum pH range 7.0-8.5) and preferentially hydrolysed p-nitroanilides containing hydrophobic amino acids
Nataša Bozic +2 more
exaly +6 more sources
The major leucyl aminopeptidase (LAP) from the midgut of Morimus funereus larvae was purified and characterised. Specific LAP activity was increased 292-fold by purification of the crude midgut extract. The purified enzyme had a pH optimum of 7.5 (optimum pH range 7.0-8.5) and preferentially hydrolysed p-nitroanilides containing hydrophobic amino acids
Nataša Bozic +2 more
exaly +6 more sources
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 (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
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
openaire +2 more sources
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
openaire +2 more sources
Leucyl/Cystinyl Aminopeptidase Gene Variants in Septic Shock
Chest, 2011Vasopressin 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 +9 more
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