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Wataru Nishii et al.
Biochemical and biophysical research communications, 301(4), 1023-1029 (2003-02-19)
Previously, we purified and partially characterized physarolisin, a lysosomal acid proteinase from Physarum polycephalum, which had been suggested to be concerned with the morphological changes of the mold. In this study, a cDNA for the enzyme was cloned and sequenced
Ostrich pepsins I and II: a kinetic and thermodynamic investigation.
B I Pletschke et al.
The international journal of biochemistry & cell biology, 27(12), 1293-1302 (1995-12-01)
G Iliadis et al.
FEBS letters, 352(3), 315-317 (1994-10-03)
Fourier transform (FTIR) difference spectra of pepsin minus diazoacetylnorleucine methyl ester (DAN) or minus diazoacetyl-L-phenylalanine methyl ester (DAP) modified pepsin, respectively, demonstrated that Asp-215 is not deprotonated in pepsin. The FTIR difference spectrum of pepsin minus 1,2-epoxyparanitrophenoxypropane (EPNP) modified pepsin
S K Ackerman et al.
Biochimica et biophysica acta, 629(3), 470-481 (1980-05-22)
Treatment of human neutrophils with a reagent (diazoacetylnorleucine methyl ester plus copper ion) which covalently labels the active site of the acid proteases, pepsin and cathepsin D, inhibits neutrophil chemotaxis and enzyme release stimulated by the chemoattractants pepstatin and formylmethiony
Elizabeth Valdivieso et al.
Experimental parasitology, 116(1), 77-82 (2006-11-28)
An aspartyl proteinase activity was detected in the soluble fraction (SF) of Leishmania mexicana promastigotes by the use of the synthetic substrate benzoyl-Arg-Gly-Phe-Phe-Leu-4-methoxy-beta-naphthylamide selective for Cathepsin D like aspartyl-proteinases. This peptide was hydrolyzed with an apparent K(m) of 2.3+/-0.3 microM.
Senarath B P Athauda et al.
The Biochemical journal, 399(3), 535-542 (2006-07-04)
The wild type Copia Gag precursor protein of Drosophila melanogaster expressed in Escherichia coli was shown to be processed autocatalytically to generate two daughter proteins with molecular masses of 33 and 23 kDa on SDS/PAGE. The active-site motif of aspartic
L Rupova et al.
Zeitschrift fur Parasitenkunde (Berlin, Germany), 61(1), 83-91 (1979-01-01)
A new protease, detected in an extract of Fasciola hepatica, was isolated and partly purified. The pH optimum for the cleavage of denaturated haemoglobin by the enzyme is pH 3.0. This proteolytic activity is inhibited by diazoacetylnorleucine methyl ester, pepstatin
S Kennedy et al.
Journal of dental research, 77(7), 1515-1519 (1998-07-15)
Whole human saliva contains a number of proteolytic enzymes, mostly derived from white blood cells and bacteria in the oral cavity. However, less information is available regarding proteases produced by salivary glands and present in salivary secretions. In the present
M Prescott et al.
The international journal of biochemistry & cell biology, 27(7), 729-739 (1995-07-01)
An acid proteinase, Wai 21a, produced by a thermophilic Bacillus species (strain Wai 21a) has been purified to homogeneity by cation-exchange chromatography, phenyl-Sepharose chromatography and anion-exchange chromatography. A pI of 3.8 was determined by isoelectric focussing. The protein contained some
Senarath B P Athauda et al.
The Biochemical journal, 381(Pt 1), 295-306 (2004-03-24)
Carnivorous plants are known to secrete acid proteinases to digest prey, mainly insects, for nitrogen uptake. In the present study, we have purified, for the first time, to homogeneity two acid proteinases (nepenthesins I and II) from the pitcher fluid
K Oda et al.
Journal of biochemistry, 128(3), 499-507 (2000-08-31)
Kumamolysin, a carboxyl proteinase from Bacillus novosp. MN-32, is characterized by its thermostability and insensitivity to aspartic proteinase inhibitors such as pepstatin, diazoacetyl-DL-norleucine methylester, and 1,2-epoxy-3-(p-nitro-phenoxy)propane. Here, its substrate specificity was elucidated using two series of synthetic chromogenic substrates: P(5)-P(4)-P(3)-P(2)-Phe*Nph
I Katoh et al.
Nature, 329(6140), 654-656 (1987-10-15)
Retrovirus protease is an enzyme that cleaves gag and gag-pol precursor polyproteins into the functional proteins of mature virus particles. The correct processing of precursor polyproteins is necessary for the infectivity of virus particles: in vitro mutagenesis which introduces deletions
A S Brecher et al.
Fundamental & clinical pharmacology, 13(1), 107-112 (1999-02-23)
Chicken egg white lysozyme is progressively inhibited by diazoacetyl-DL-norleucine methyl ester (DANME) and by chlorambucil at concentrations of 3.4 x 10(-3) M and 5 x 10(-3) M respectively over a three-hour time period. DANME inhibits lysozyme activity to the extent
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