alpha-chymotrypsin has been researched along with fluorophosphate* in 7 studies
7 other study(ies) available for alpha-chymotrypsin and fluorophosphate
| Article | Year |
|---|---|
A serine alkaline protease from the fungus Conidiobolus coronatus with a distinctly different structure than the serine protease subtilisin Carlsberg.
In view of the functional similarities between subtilisin Carlsberg and the alkaline protease from Conidiobolus coronatus, the biochemical and structural properties of the two enzymes were compared. In spite of their similar biochemical properties, e.g., pH optima, heat stability, molecular mass, pI, esterase activity, and inhibition by diisopropyl fluorophosphate and phenylmethlysulfonylfluoride, the proteases were structurally dissimilar as revealed by (1) their amino acid compositions, (2) their inhibition by subtilisin inhibitor, (3) their immunological response to specific anti-Conidiobolus protease antibody, and (4) their tryptic peptide maps. Our results demonstrate that although they are functionally analogous, the Conidiobolus protease is structurally distinct from subtilisin Carlsberg. The Conidiobolus protease was also different from other bacterial and animal proteases (e.g. pronase, protease K, trypsin, and chymotrypsin) as evidenced by their lack of response to anti-Conidiobolus protease antibody in double diffusion and in neutralization assays. The Conidiobolus serine protease fails to obey the general rule that proteins with similar functions have similar primary sequences and, thus, are evolutionarily related. Our results strengthen the concept of convergent evolution for serine proteases and provide basis for research in evolutionary relationships among fungal, bacterial, and animal proteases. Topics: Amino Acids; Antibodies, Fungal; Chymotrypsin; Endopeptidase K; Entomophthora; Fluorides; Hot Temperature; Hydrogen-Ion Concentration; Neutralization Tests; Peptide Mapping; Phosphates; Phylogeny; Pronase; Serine Endopeptidases; Serine Proteinase Inhibitors; Subtilisins; Trypsin | 1996 |
CHARACTERIZATION OF A REVERSIBLY FORMED ENZYME COMPLEX IN THE REACTION OF CHYMOTRYPSIN WITH DIISOPROPYL FLUOROPHOSPHATE.
Topics: Chemical Phenomena; Chemistry; Chymotrypsin; Fluorides; Hydrogen-Ion Concentration; Isoflurophate; Kinetics; Multienzyme Complexes; Phenylalanine; Phosphates; Research; Spectrophotometry | 1965 |
The inhibition of beta- and gamma-chymotrypsin and trypsin by diisopropyl fluorophosphate.
Topics: Chymotrypsin; Endopeptidases; Fluorides; Humans; Isoflurophate; Peptide Hydrolases; Phosphates; Trypsin Inhibitors | 1952 |
Reaction of alpha-chymotrypsin with analogues of diisopropyl fluorophosphate.
Topics: Chymotrypsin; Fluorides; Isoflurophate; Organic Chemicals; Phosphates | 1951 |
Mode of inhibition of chymotrypsin by diisopropyl fluorophosphate. II. Introduction of isopropyl and elimination of fluorine as hydrogen fluoride.
Topics: Biological Transport; Chymotrypsin; Fluorides; Fluorine; Hydrofluoric Acid; Isoflurophate; Phosphates | 1950 |
Inhibition of the proteinase and esterase activities of trypsin and chymotrypsin by diisopropyl fluorophosphate; crystallization of inhibited chymotrypsin.
Topics: Chymotrypsin; Crystallization; Endopeptidases; Esterases; Fluorides; Humans; Isoflurophate; Phosphates; Trypsin | 1949 |
Mode of inhibition of chymotrypsin by diisopropyl fluorophosphate; introduction of phosphorus.
Topics: Chymotrypsin; Fluorides; Isoflurophate; Phosphates; Phosphorus | 1949 |