Results 121 to 130 of about 8,434 (154)
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Placental Leucine Aminopeptidase
2004Human pregnancy serum and placenta are known to have the ability to degrade oxytocin (OT), the most potent uterotonic peptide. Placental leucine aminopepetidase (P-LAP), which is also called cystine aminopeptidase, is the only membrane aminopeptidase known to open the N-terminal cystine loop of OT. The soluble form of P-LAP present in maternal serum is
Seiji Nomura +2 more
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American Journal of Diseases of Children, 1962
Histochemical studies of adult liver for leucine aminopeptidase (LAP) utilizing the synthetic substrate L-leucyl-β-naphthylamide show intense activity in the bile duct epithelium and a weaker reaction in the parenchymal cells.1,2We have also observed high activity in the proliferating bile ducts of liver biopsies from 4 infants with biliary atresia ...
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Histochemical studies of adult liver for leucine aminopeptidase (LAP) utilizing the synthetic substrate L-leucyl-β-naphthylamide show intense activity in the bile duct epithelium and a weaker reaction in the parenchymal cells.1,2We have also observed high activity in the proliferating bile ducts of liver biopsies from 4 infants with biliary atresia ...
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Leucine aminopeptidase: A zinc metalloenzyme
Archives of Biochemistry and Biophysics, 1969Abstract The leucine aminopeptidase of the supernatant fraction of porcine kidney is instantaneously inhibited by orthophenanthroline, bipyridyl, cupferron, sodium diethyldithiocarbamide, sodium sulfide, and sodium cyanide. All of these inhibitions are reversed by addition of group IIb metal ions in appropriate quantity to the reaction mixture ...
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Genetics of leucine aminopeptidase in apple
Theoretical and Applied Genetics, 1992Six zones of LAP activity were detected in apples, some of them tissue specific. Genetic studies in four of them revealed the presence of four genes LAP-1, LAP-2, LAP-3 and LAP-4 with 4, 5, 4 and 4 alleles respectively including two null alleles. There were no big differences in allelic frequency within cultivars, selections, rootstocks and Malus ...
A G, Manganaris, F H, Alston
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Leucine Aminopeptidase Activity in Infectious Hepatitis
Archives of Pediatrics & Adolescent Medicine, 1963Leucine aminopeptidase (LAP) is a proteolytic enzyme which is present in human blood serum. Its serum concentration is usually elevated in disease of the hepatobiliary system. Banks et al. 1 have described the clinical value of measuring LAP activity. More recently, Rutenburg et al.
J P, GILES +4 more
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Leucine Aminopeptidase Activity in Mast Cells
Nature, 1959DURING investigations of the behaviour of leucine aminopeptidase activity of blood-serum in patients with dermatoses and tumours1–3, in a case of diffuse skin mastocytosis of a new-born, we detected heightened activity of leucine aminopeptidase. After mechanical friction of the affected skin, greater activity of leucine aminopeptidase occurred.
O, BRAUN-FALCO, K, SALFELD
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Journal of Biochemistry, 1999
In the current study, we report the cloning and initial characterization of a novel human cytosolic aminopeptidase named adipocyte-derived leucine aminopeptidase (A-LAP). The sequence encodes a 941-amino acid protein with significant homology (43%) to placental leucine aminopeptidase (P-LAP)/oxytocinase.
A, Hattori +3 more
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In the current study, we report the cloning and initial characterization of a novel human cytosolic aminopeptidase named adipocyte-derived leucine aminopeptidase (A-LAP). The sequence encodes a 941-amino acid protein with significant homology (43%) to placental leucine aminopeptidase (P-LAP)/oxytocinase.
A, Hattori +3 more
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[Leucine aminopeptidase (LAP)].
Rinsho byori. The Japanese journal of clinical pathology, 2002We regarded the aminopeptidase LAP (EC 3.4.11.1), AA (EC 3.4.11.2), and CAP (EC 3.4.11.3) as a group of enzymes and presented the method of their fractionation. In addition, we described that when an increase in serum "LAP" activity is observed, it is necessary to consider whether it is derived from LAP, AA, or CAP in order to use that data in clinical
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Comparison of leucine aminopeptidase and aminopeptidase III activities in lens
Current Eye Research, 1996To evaluate the relative contribution of leucine aminopeptidase and aminopeptidase III activities to the total aminopeptidase activity in bovine and human lenses under in vivo pH conditions.Bovine and human lens extracts were fractionated on a Sephadex G-200 column at pH 6.9 and 8.5 and all the fractions were assayed with Leu-pNA and Arg-pNA as ...
K K, Sharma, N J, Elser, K, Kester
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The thiolesterase activity of leucine aminopeptidase
Biochimica et Biophysica Acta (BBA) - Enzymology, 1972Abstract 1. 1. Leucine aminopeptidase ( l -leucyl-peptide hydrolase, EC 3.4.1.1) has been shown to be capable of hydrolyzing leucine thiol ethyl ester at a rate 50 times greater than the rate for l -leucine-p-nitroanilide. 2. 2. The pH optimum for the reaction is 8.6 and the Km is 1.3·10−3 M. 3. 3.
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