Results 101 to 110 of about 1,233 (154)
Abstract The food enzyme leucyl aminopeptidase (EC 3.4.11.1) is produced with the genetically modified Aspergillus oryzae strain NZYM‐BU by Novozymes A/S. The safety of this food enzyme was evaluated previously, and it did not give rise to safety concerns when used in five food manufacturing processes.
EFSA Panel on Food Enzymes (FEZ) +15 more
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Role of Aminopeptidase in Angiogenesis
Microvessels are composed of endothelial cells and surrounding pericytes. Angiogenesis, a neo-vessel formation from pre-existing microvessels, is a complex phenomenon, which requires following sequential steps: detachment of pre-existing pericytes for vascular destabilization, extracellular matrix turnover, migration, proliferation, tube formation by ...
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Chromogenic Substrates for Aminopeptidase.
SummaryChromogenic aminopeptides have been synthesized which are readily hydrolyzed by extracts of human tissues and human serum, duodenal juice and urine. It is possible to localize enzymatic activity histochemically by the use of these substrates.
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Immobilized Derivatives of Leucine Aminopeptidase and Aminopeptidase M
Garfield P. Royer, John P. Andrews
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THE SPECIFICITY OF LEUCINE AMINOPEPTIDASE
E L, SMITH, N B, SLONIM
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Aminopeptidase A in human placenta
Biochimica et Biophysica Acta (BBA) - Enzymology, 1981Abstract Aminopeptidase A ( l -α-aspartyl( l -α-glutamyl)-peptide hydrolase, EC 3.4.11.7) was found in human placenta, partially purified from it and briefly characterized in comparison with the placental leucine aminopeptidase. The aminopeptidase A could be separated from leucine aminopeptidase after trypsin digestion followed by Sephacryl S-300 ...
S, Mizutani +4 more
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Dipeptidyl-aminopeptidases and aminopeptidases in Dictyostelium discoideum
Biochemical and Biophysical Research Communications, 1985Extracts prepared from culminating cells of Dictyostelium discoideum have been found to contain dipeptidyl-aminopeptidases I (EC 3.4.14.1), II (EC 3.4.14.2), III (EC 3.4.14.4), arginine aminopeptidase (EC 3.4.11.6) and valine aminopeptidase. Dipeptidyl-aminopeptidase III was the most active of the dipeptidyl-aminopeptidases; its molecular weight was ...
S A, Chan +3 more
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Histochemistry, 1980
A comparative biochemical and histochemical investigation of aminopeptidase A (APA, E.C. 3.4.11.7) was carried out. α-Glu-1NA, α-Glu-2NA, α-Glu-MNA and Asp-2NA were used as substrates, Fast Blue B (FBB), hexazotized new fuchsin (HNF) and hexazonium-p-rosaniline (HPR) as coupling agents.
Z, Lojda, R, Gossrau
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A comparative biochemical and histochemical investigation of aminopeptidase A (APA, E.C. 3.4.11.7) was carried out. α-Glu-1NA, α-Glu-2NA, α-Glu-MNA and Asp-2NA were used as substrates, Fast Blue B (FBB), hexazotized new fuchsin (HNF) and hexazonium-p-rosaniline (HPR) as coupling agents.
Z, Lojda, R, Gossrau
openaire +2 more sources

