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Diazoacetyl-DL-norleucine methyl ester


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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
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
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

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