Results 111 to 120 of about 1,804 (142)
Some of the next articles are maybe not open access.
The leucyl aminopeptidase from Helicobacter pylori is an allosteric enzyme
Microbiology, 2005This 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 +5 more
openaire +2 more sources
Biophysical characterization of a recombinant leucyl aminopeptidase from Bacillus kaustophilus
Biochemistry (Moscow), 2010The 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 +5 more
openaire +2 more sources
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 +3 more
openaire +2 more sources
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 +3 more
openaire +2 more sources
Effect of tuftsin on leucyl aminopeptidase activity of subcellular components of the cerebral cortex
Bulletin of Experimental Biology and Medicine, 1989exaly +2 more sources
Journal of Basic Microbiology, 1997
AbstractVarious methods for the isolation of periplasm were examined and compared with regard to the complete release of known periplasmic marker enzymes and the contamination of the periplasm by cytosol for Pseudomonas aeruginosa PAO1 as a significant Gram‐negative test strain.
T, Jensch, B, Fricke
openaire +2 more sources
AbstractVarious methods for the isolation of periplasm were examined and compared with regard to the complete release of known periplasmic marker enzymes and the contamination of the periplasm by cytosol for Pseudomonas aeruginosa PAO1 as a significant Gram‐negative test strain.
T, Jensch, B, Fricke
openaire +2 more sources
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 +7 more
openaire +2 more sources
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 +7 more
openaire +2 more sources
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 +4 more
openaire +2 more sources
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 +4 more
openaire +2 more sources
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 +3 more
openaire +2 more sources
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 +3 more
openaire +2 more sources
Prolyl aminopeptidase from rat brain and kidney
European Journal of Biochemistry, 1990Based 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
Theoretical and Applied Genetics, 1982
A gene termed gpiB, coding for one of the two isoenzyme zones of glucose phosphate isomerase in Petunia, has been mapped to a locus on chromosome VII by means of linkage to the marker An4, and by an allelic dosage effect on enzyme activity in trisomics.
H J, Wijsman, B M, van den Berg
openaire +2 more sources
A gene termed gpiB, coding for one of the two isoenzyme zones of glucose phosphate isomerase in Petunia, has been mapped to a locus on chromosome VII by means of linkage to the marker An4, and by an allelic dosage effect on enzyme activity in trisomics.
H J, Wijsman, B M, van den Berg
openaire +2 more sources