Results 151 to 160 of about 3,849 (186)

Purification and properties of major midgut leucyl aminopeptidase of Morimus funereus (Coleoptera, Cerambycidae) larvae

Comparative Biochemistry and Physiology Part 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
Bozić, Natasa M, Ivanović, Jelisaveta, Nenadović, Vera, Bergstroem, Joergen, Larsson, Thomas, Vujčić, Zoran M.   +5 more
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Changes of arginyl and leucyl aminopeptidase activities in biceps femoris along Jinhua ham processing

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 M, Zhao, Y L, Wang, W, Tian, G H, Zhou, X L, Xu, Y X, Liu   +5 more
openaire   +4 more sources

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
openaire   +2 more sources

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
openaire   +2 more sources

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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Human brain leucyl aminopeptidase: Isolation, characterization and specificity against some neuropeptides

Neuropeptides, 1991
In order to obtain a greater understanding of the role of aminopeptidases in the degradation of peptides and proteins in the nervous system, we have isolated and characterized leucyl aminopeptidase (EC 3.4.11.1) from human cerebral cortex and studied its action on some physiologically important neuropeptides.
A M, Gibson, J A, Biggins, B, Lauffart, D, Mantle, J R, McDermott   +4 more
openaire   +2 more sources

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
openaire   +2 more sources

The colorimetric determination of leucine aminopeptidase activity with l-leucyl-β-naphthylamide hydrochloride

Archives of Biochemistry and Biophysics, 1955
Abstract The synthesis of l -leucine-β-naphthylamide hydrochloride as a colorimetric substrate for the determination of leucine aminopeptidase is described along with the synthesis of optical isomers and other derivatives designed to clarify the specificity of the substrate.
M N, GREEN, K C, TSOU, R, BRESSLER, A M, SELIGMAN   +3 more
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Prolyl aminopeptidase from rat brain and kidney

European Journal of Biochemistry, 1990
Based on the liberation of proline from ProLeuGlyNH2 (MIF‐1, melanostatin) manganese‐activated prolyl aminopeptidase activities were purified from rat brain and kidney cytosolic fractions. They were distinguished from other di‐ and tripeptidases and an arylamidase liberating N‐terminal proline.
A, Turzynski, R, Mentlein
openaire   +2 more sources

Puromycin insensitive leucyl‐specific aminopeptidase (PILSAP) is involved in the activation of endothelial integrins

Journal of Cellular Physiology, 2002
AbstractWe previously reported that mouse orthologue of puromycin insensitive leucyl‐specific aminopeptidase (mPILSAP) played an important role in angiogenesis by regulating the proliferation and migration of endothelial cells (ECs) (Miyashita et al., 2002. Blood 99:3241–3249).
Tetsuya, Akada, Tohru, Yamazaki, Hiroki, Miyashita, Osamu, Niizeki, Mayumi, Abe, Akira, Sato, Susumu, Satomi, Yasufumi, Sato   +7 more
openaire   +2 more sources