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" within Papers

Structural and enzymatic characterization of physarolisin (formerly physaropepsin) proves that it is a unique serine-carboxyl proteinase.

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)

Aspartic proteinases--Fourier transform IR studies of the aspartic carboxylic groups in the active site of pepsin.

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

Neutrophil chemotaxis and enzyme release competitive inhibition by a diazoacetamide pepsin inhibitor.

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

Leishmania mexicana: identification and characterization of an aspartyl proteinase activity.

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.

Isolation and characterization of recombinant Drosophila Copia aspartic proteinase.

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

Isolation and some properties of an acid protease from Fasciola hepatica.

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

Submandibular salivary proteases: lack of a role in anti-HIV activity.

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

Characterisation of a thermostable pepstatin-insensitive acid proteinase from a Bacillus sp.

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

Enzymic and structural characterization of nepenthesin, a unique member of a novel subfamily of aspartic proteinases.

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

Subsite preferences of pepstatin-insensitive carboxyl proteinases from prokaryotes: kumamolysin, a thermostable pepstatin-insensitive carboxyl proteinase.

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

Inhibition of retroviral protease activity by an aspartyl proteinase inhibitor.

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

The effect of chlorambucil upon lysozyme activity.

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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