alpha-chymotrypsin and 4-(4-dimethylaminophenylazo)benzoic-acid

alpha-chymotrypsin has been researched along with 4-(4-dimethylaminophenylazo)benzoic-acid* in 1 studies

Other Studies

1 other study(ies) available for alpha-chymotrypsin and 4-(4-dimethylaminophenylazo)benzoic-acid

Article	Year
Proteolytic stability of beta-peptide bonds probed using quenched fluorescent substrates incorporating a hemoglobin cleavage site. FEBS letters, 2003, Jan-30, Volume: 535, Issue:1-3 A set of designed internally quenched fluorescence peptide substrates has been used to probe the effects of insertion of beta-peptide bonds into peptide sequences. The test sequence chosen corresponds to a proteolytically susceptible site in hemoglobin alpha-chain, residues 32-37. Fluorescence and mass spectral measurements demonstrate that the insertion of an beta-residues at the potential cleavage sites completely abolishes the action of proteases; in addition, the rate of cleavage of the peptide bond preceding the site of modification is also considerably reduced. Topics: Animals; Aspartic Acid Endopeptidases; Binding Sites; Chymotrypsin; Endopeptidase K; Fluorescent Dyes; Hemoglobins; Naphthalenesulfonates; p-Dimethylaminoazobenzene; Pepsin A; Peptides; Plasmodium falciparum; Protozoan Proteins; Spectrometry, Fluorescence; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Substrate Specificity; Trypsin	2003

Article

Year

Proteolytic stability of beta-peptide bonds probed using quenched fluorescent substrates incorporating a hemoglobin cleavage site.

FEBS letters, 2003, Jan-30, Volume: 535, Issue:1-3

A set of designed internally quenched fluorescence peptide substrates has been used to probe the effects of insertion of beta-peptide bonds into peptide sequences. The test sequence chosen corresponds to a proteolytically susceptible site in hemoglobin alpha-chain, residues 32-37. Fluorescence and mass spectral measurements demonstrate that the insertion of an beta-residues at the potential cleavage sites completely abolishes the action of proteases; in addition, the rate of cleavage of the peptide bond preceding the site of modification is also considerably reduced.

Topics: Animals; Aspartic Acid Endopeptidases; Binding Sites; Chymotrypsin; Endopeptidase K; Fluorescent Dyes; Hemoglobins; Naphthalenesulfonates; p-Dimethylaminoazobenzene; Pepsin A; Peptides; Plasmodium falciparum; Protozoan Proteins; Spectrometry, Fluorescence; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Substrate Specificity; Trypsin

2003