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Cathepsin S and Cruzipain Are Inhibited by Equistatin from Actinia equina
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V. Stoka
Published/Copyright:
June 1, 2005
Abstract
Cathepsin S has been isolated for the first time from human tissue. It has a molecular mass of 24 kDa and an isoelectric point in the range of 8.2 to 8.6. The enzyme is inhibited by equistatin, which belongs to the thyropins, a new family of protein inhibitors, with an inhibition constant of Ki = 0.40 ± 0.07nm. Cruzipain, a cathepsin L-like enzyme sharing a 130 amino acid long C-terminal extension, is also strongly inhibited by equistatin (Ki = 0.028 ± 0.006nm). Together with previously reported data, these results further indicate that a functional heterogeneity exists among thyropin inhibitors, as demonstrated by their interaction with cathepsin S and cruzipain.
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Published Online: 2005-06-01
Published in Print: 1999-05-03
Copyright ©1999 by Walter de Gruyter GmbH & Co. KG
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Articles in the same Issue
- Biosynthesis of Glycosylphosphatidylinositols in Mammals and Unicellular Microbes
- Activation of DNA Replication in Yeast by Recruitment of the RNA Polymerase II Transcription Complex
- On the Role of Symmetrical and Asymmetrical Chaperonin Complexes in Assisted Protein Folding
- Regulation of Cathepsin B Activity by Cysteine and Related Thiols
- Epitope Mapping of the Monoclonal Antibody MM12.10 to External MDR1 P-Glycoprotein Domain by Synthetic Peptide Scanning and Phage Display Technologies
- Molecular Mimicry between a Monoclonal Antibody and One Subunit of Crotoxin, a Heterodimeric Phospholipase A2 Neurotoxin
- Enzyme-Linked Immunosorbent Assay for the Measurement of JNK Activity in Cell Extracts
- Mitochondrial DNA Acts as Potential Promoter of the Baculovirus RNA Polymerase
- In Vitro Phosphorylation of Purified Glycosylphos-phatidylinositol-Specific Phospholipase D
- Cathepsin S and Cruzipain Are Inhibited by Equistatin from Actinia equina
- Lipopeptides as Dimerization Inhibitors of HIV-1 Protease
