Results 111 to 120 of about 1,860 (145)
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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
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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
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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
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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
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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
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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
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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
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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
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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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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
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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 +5 more
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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 +5 more
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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
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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
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[Comparison between leucyl aminopeptidase and pseudo leucine aminopeptidase activities in sera].
Rinsho byori. The Japanese journal of clinical pathology, 2000The highest activities of leucyl aminopeptidase(LAP, cytosol aminopeptidase, EC 3.4.11.1) in sera have been found in patients with acute hepatitis(Kanno et al., Am J Clin Path, 82: 700-705, 1984). I observed inpatients with very high activities of LAP and alcohol dehydrogenase(AD) in sera.
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