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Proteolytic activity of pseudotrypsin
An observed proteolytic action and specificity of pseudotrypsin is reported and its ability to bind basic pancreatic trypsin inhibitor (BPTI) is reported on. Expand
Chemical and enzymatic characterization of the collagenase from the insect Hypoderma lineatum.
The amino acid composition of Hypoderma collagenase indicates a distinct similarity with the serine proteinases of the trypsin family and with another athropode serine collagenase, that of the fiddler crab Uca pugilator, which suggests that eucaryotic collagenases with digestive rather than morphogenic function represent a new category of members of thetrypsinFamily. Expand
Specificity of the collagenase from the insect Hypoderma lineatum.
Hypoderma collagenase differs from proteinases I and II from the crab Uca pugilator, which catalyse cleavages in multiple regions of the collagen molecule, and also from vertebrate collagenases, which cleave collagen only between residues 775 and 776. Expand
Hypodermin A, a trypsin-like neutral proteinase from the insect Hypoderma lineatum.
Sequence analysis suggests structural homology with H. lineatum collagenase as well as with other members of the trypsin family in Hypodermin A, a serine proteinase from the larva Hypoderma lineatum. Expand
Complete amino acid sequence of the collagenase from the insect Hypoderma lineatum.
The primary structure of the Hypoderma lineatum collagenase was determined and thermolysin fragmentation of the chymotryptic core gave 30 and 5 peptides, respectively, accounting for all the residues of the protein. Expand
Proteolysis Data Bank: specificity of alpha-chymotrypsin from computation of protein cleavages.
  • B. Keil
  • Chemistry, Medicine
  • Protein sequences & data analysis
  • 1987
The results of the study indicate that predictions of cleavage by proteolytic enzymes can be made from the sequence of polypeptide substrates, provided that a sufficient pool of experimental data has been collected. Expand
Specificity of the collagenolytic enzyme from the fungus Entomophthora coronata: comparison with the bacterial collagenase from Achromobacter iophagus.
The fungal collagenolytic enzyme from Entomophthora coronata differs both structurally and functionally from the bacterial Achromobacter collagenase. Expand
alpha-Clostripain. Chemical characterization, activity, and thiol content of the highly active form of clostripain.
A highly active form of clostripain, composed of two polypeptide chains (Mr = 43,000 and 12,500), was isolated by hydrophobic chromatography from the culture medium of Clostridium histolyticum. ItExpand
Differences in the degradation of native collagen by two microbial collagenases.
The purified collagenase from Clostridium histolyticum was shown to cleave native collagen at several sites, but not progressively from the N-terminus, as had been previously suggested. Expand
Proteolytic enzymes of Entomophthora coronata. Characterization of a collagenase
A collagenase which degrades specifically helical regions of native collagen has been separated from a BAE-esterase and a component with carboxypeptidase activity is associated with the collagenolytic activity. Expand