Results 121 to 130 of about 8,618 (173)
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Comparison of leucine aminopeptidase and aminopeptidase III activities in lens

Current Eye Research, 1996
To 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 Krishna Sharma
exaly   +3 more sources

Genetics of leucine aminopeptidase in apple

Theoretical and Applied Genetics, 1992
Six 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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Electron microscopy of leucine aminopeptidase

Journal of Molecular Biology, 1977
Abstract Electron microscopy of negatively stained preparations of leucine aminopeptidase in solution revealed a few distinctive types of particle image. Analysis of these images and of their variants allows us to propose a model for LAPase † : six subunits are arranged with 32 symmetry at the vertices of a distorted triangular prism (the structure
N A, Kiselev   +4 more
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Leucine aminopeptidase: A zinc metalloenzyme

Archives of Biochemistry and Biophysics, 1969
Abstract 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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The thiolesterase activity of leucine aminopeptidase

Biochimica et Biophysica Acta (BBA) - Enzymology, 1972
Abstract 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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Serum Leucine Aminopeptidase

American Journal of Diseases of Children, 1963
Introduction A great deal of information has accumulated in the past few years concerning the activity of the enzyme, serum leucine aminopeptidase (LAP) in physiologic and pathologic states. With the exception of a rise in LAP activity occurring during pregnancy, 1 an elevation in LAP activity is almost exclusively associated with diseases of the ...
openaire   +1 more source

Placental Leucine Aminopeptidase

2004
Human 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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Serum Leucine Aminopeptidase

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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Leucine aminopeptidase during meiotic development

European Journal of Biochemistry, 2002
We found a leucine aminopeptidase (LAP; EC 3.4.11.1) to be abundant in meiotic prophase tissue of a basidiomycete, Coprinus cinereus. After direct purification of the aminopeptidase component from meiocytes, we cloned the gene by degenerate PCR using partial amino‐acid sequences of the purified enzyme and 5′ and 3′ RACE.
Takashi, Ishizaki   +8 more
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Leucine aminopeptidase in the foetal kidney of the rat

Experientia, 1961
Histochemisch demonstrierbare Leucinaminopeptidase erschien in den letzten Tagen der Schwangerschaft in einzelnen Gruppen von Tubuli der Rinde der fotalen Rattenniere. Der grosste Teil der Rinde und das Mark erwiesen sich als negativ. Nach der Geburt verbreitete sich das Ferment uber die ganze Rinde und vermehrte seine Aktivitat stark.
V K, HOPSU, S, RUPONEN, S, TALANTI
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