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Crystal structure of porcine cathepsin H determined at 2.1 A resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function.
The crystal structure of cathepsin H reveals that themini-chain has a definitive role in substrate recognition and that carbohydrate residues attached to the body of the enzyme are involved in positioning the mini-chain in the active-site cleft.
The preparation of catalytically active human cathepsin B from its precursor expressed in Escherichia coli in the form of inclusion bodies.
A cDNA clone encoding human procathepsin B was expressed at a high level in Escherichia coli using a T7 polymerase expression system, resulting in the formation of insoluble cytoplasmic protein
Equinatoxins, pore-forming proteins from the sea anemone Actinia equina, belong to a multigene family.
The cDNA sequence of a new, sphingomyelin inhibited equinatoxin, EqtIV, is reported, confirming two isoforms of EqtI, differing at position 13, indicating that Eqts belong to a multigene family.
Recombinant lamb chymosin as an alternative coagulating enzyme in cheese production.
The temperature instability of RLC at temperatures above 45 degrees C could constitute a benefit in making hard cheese varieties and the overall quality of the cheese was at least comparable to that of the cheeses made with RCC, and both cheeses were better scored than the cheese made with CR.
Glycosaminoglycans Facilitate Procathepsin B Activation through Disruption of Propeptide-Mature Enzyme Interactions*
It is demonstrated that polyanionic polysaccharides, glycosaminoglycans (GAGs), can accelerate the autocatalytic removal of the propeptide and subsequent activation of cathepsin B.
Cloning, sequencing, and expression of equinatoxin II.
Recombinant toxin was isolated by a simple, two-step isolation procedure including separation on CM-cellulose and gel filtration using an FPLC system and its biochemical properties and hemolytic activity were practically indistinguishable from those of native toxin.
Stefins and lysosomal cathepsins B, L and D in human breast carcinoma
In the study of 50 matched pairs of breast carcinoma and normal breast tissue, the activities of cysteine proteinases, cathepsin (Cat) B and Cat L in tumors were increased on average by 18.5‐fold and 52.5-fold, and it was suggested that lowered CPI might rather reflect changes in transcription of intracellular CPIs, the stefins.
Cysteine-scanning mutagenesis of an eukaryotic pore-forming toxin from sea anemone: topology in lipid membranes.
The overall results suggest that at least two regions are embedded within the lipid membrane: the N-terminal 13-20 region, probably forming an amphiphilic helix, and the tryptophan-rich 105-120 region that could be involved in making contacts with lipid headgroups.
Autocatalytic processing of procathepsin B is triggered by proenzyme activity
A model for autocatalytic activation of cysteine cathepsins is proposed, involving propeptide dissociation from the active‐site cleft as the first step during zymogen activation.