Thyroglobulin, the precursor of thyroid hormones, is extracellularly stored in a highly condensed and covalently cross-linked form. Solublization of thyroglobulin is facilitated by cysteine proteinases like cathepsins B and K which are proteolytically active at the surface of thyroid epithelial cells. The cysteine proteinases mediate the processing of thyroglobulin by limited extracellular prot...

We deduced that Agkistrodon actus venom serine proteinases I and II, previously isolated from the venom of A. acutus (Zhu, Z., Gong, P., Teng, M., and Niu, L. (2003) Acta Crystallogr. Sect. D Biol. Crystallogr. 59, 547-550), are encoded by two almost identical genes, with only the single substitution Asp for Asn at residue 62. Amidolytic assays indicated that they possess slightly different enz...

Background-A recent report demonstrated the immunogenic character of the cysteine proteinases of Trichomonas vaginalis. It was of interest, therefore, to examine for the presence of serum anti-proteinase antibody among patients with trichomoniasis. Methods-An immunoprecipitation assay was used involving protein A-bearing Staphylococcus aureus first coated with the IgG fraction ofgoat anti-human...

Activation of the Hageman factor-kallikrein-kinin system by serratial 56-kDa proteinase was previously demonstrated (Matsumoto, K., Yamamoto, T., Kamata, T., and Maeda, H. (1984) J. Biochem. (Tokyo) 96, 739-749; Kamata, R., Yamamoto, T., Matsumoto, K., and Maeda, H. (1985) Infect. Immun. 48, 747-753). To investigate whether the activation of the system is specific for 56-kDa proteinase or is fo...

Although the production of proteolytic enzymes by different strains of Aspergillus oryzae has been investigated in submerged culture (5, 15), in static liquid culture (3, 11), and on solid substratum (8-10), there appear to be few reports pertaining to the comparative evaluation of these different methods on the elaboration of proteinases by specific strains of A. oryzae. K. Mogi (13) compared ...

Specific inhibitors of three lysosomal proteinases are present in the cytosolic and lysosomal compartments of rabbit liver. The cytosolic inhibitors, purified by chromatography on DEAE-Trisacryl and Sephadex G-75, show specificities toward cathepsin M, cathepsins B and L, and fructose 1,6-bisphosphatase converting enzyme (CE), respectively, and are designated IM, IB/L, and ICE. Inhibitors with ...

It is now well established that the cysteine proteinases of plants (e.g. papain, actinidin, bromelain) and animals (e.g. cathepsins B, H and L) are homologous (see Takio et al., 1983) and almost certainly evolved from a common ancestral protein. For all but one of the cysteine proteinases sequenced to date the N-terminal residues can be exactly aligned with one another at a distance of 25-29 re...