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Showing 1-30 of 32 results for "C0888" within Papers
A G Breite et al.
Transplantation proceedings, 42(6), 2052-2054 (2010-08-10)
Neutral proteases, essential components of purified tissue dissociation enzymes required for successful human islet isolation, show variable activities and effects of substrate on their activities. Initially we used a spectrophotometric endpoint assay with azocasein substrate to measure neutral protease activity.
Cecilia N Arighi et al.
Biochemistry, 42(24), 7539-7551 (2003-06-18)
IFABP is a small beta-barrel protein with a short helix-turn-helix motif near the N-terminus that is thought to participate in the regulation of the uptake and delivery of fatty acids. In a previous work, we detected by near UV circular
Andrew K Ottens et al.
Journal of neurochemistry, 104(5), 1404-1414 (2007-11-27)
Neurotrauma, as in the case of traumatic brain injury, promotes protease over-activation characterized by the select fragmentation of brain proteins. The resulting polypeptides are indicators of biochemical processes, which can be used to study post-injury dynamics and may also be
Thomas J Hiscox et al.
Infection and immunity, 79(6), 2145-2153 (2011-03-16)
Clostridium perfringens causes clostridial myonecrosis or gas gangrene and produces several extracellular hydrolytic enzymes and toxins, many of which are regulated by the VirSR signal transduction system. The revR gene encodes a putative orphan response regulator that has similarity to
Hiroaki Tanaka et al.
Protein expression and purification, 76(1), 83-89 (2010-10-14)
Clostripain (CLO) produced by Clostridium histolyticum is an arginine-specific endopeptidase with the potential for applicability to diverse medical and industrial uses. In this study, we developed an expression system allowing high-level production and efficient purification of recombinant CLO (rCLO). Our
V Witte et al.
Microbiology (Reading, England), 140 ( Pt 5), 1175-1182 (1994-05-01)
Clostripain-specific antibodies were used to analyse the maturation of clostripain prepro-enzyme and core protein heterologously synthesized in Escherichia coli and Bacillus subtilis. Core protein purified from E. coli cells harbouring plasmid pHM3-23 underwent calcium-dependent, self-triggered maturation. Concomitantly, the inactive form
David T Lodowski et al.
Biochemistry, 44(18), 6958-6970 (2005-05-04)
In response to extracellular signals, G protein-coupled receptors (GPCRs) catalyze guanine nucleotide exchange on Galpha subunits, enabling both activated Galpha and Gbetagamma subunits to target downstream effector enzymes. One target of Gbetagamma is G protein-coupled receptor kinase 2 (GRK2), an
A M Gilles et al.
European journal of biochemistry, 145(3), 469-476 (1984-12-17)
The primary structure of light chain of alpha-clostripain was determined by sequence analysis of peptides derived from tryptic digests purified by reverse-phase high-performance liquid chromatography. The 22 isolated tryptic peptides were aligned by peptides derived from chymotryptic and staphylococcal V8
Chang-Kyu Kim et al.
Journal of biotechnology, 131(3), 346-352 (2007-09-05)
In this study, the clostripain gene was modified and its signal sequence was replaced with that of penicillin G acylase (PGA). The core clostripain protein fused to the PGA signal peptide was also prepared. With regard to the expression of
Nikolaos E Labrou et al.
European journal of biochemistry, 271(5), 983-992 (2004-03-11)
In this study we investigate the active-site structure and the catalytic mechanism of clostripain by using a combination of three separate techniques: affinity labelling, site-directed mutagenesis and molecular modelling. A benzamidinyl-diazo dichlorotriazine dye (BDD) was shown to act as an
Antibacterial activity of casein-derived peptides isolated from rabbit (Oryctolagus cuniculus) milk.
Maria Baranyi et al.
The Journal of dairy research, 70(2), 189-197 (2003-06-13)
Acid-precipitated rabbit 'whole casein' was digested by trypsin, chymotrypsin, pepsin, and clostripain to screen for possible peptides with antibacterial properties. The peptide fragments were separated by reversed-phase chromatography. The collected fractions were pooled and their antibacterial properties tested against Escherichia
A M Gilles et al.
The Journal of biological chemistry, 254(5), 1462-1468 (1979-03-10)
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. It differs in amino acid composition, namely in the value for cyst(e)ine
M Sawkat Anwer et al.
The Journal of biological chemistry, 280(39), 33687-33692 (2005-07-20)
Ntcp is a phosphoprotein, and its translocation by cAMP to the plasma membrane is associated with dephosphorylation. However, the phosphorylation site(s) of Ntcp is not known. Thus, the aim of the present study was to determine the potential Ntcp phosphorylation
Ozlem Doğan Ekici et al.
Journal of medicinal chemistry, 47(8), 1889-1892 (2004-04-02)
Aza-peptide Michael acceptors are a new class of irreversible inhibitors that are highly potent and specific for clan CD cysteine proteases. The aza-Asp derivatives were specific for caspases, while aza-Asn derivatives were effective legumain inhibitors. Aza-Lys and aza-Orn derivatives were
Taeko Kakizawa et al.
Bioorganic & medicinal chemistry, 19(9), 2785-2789 (2011-04-15)
A recombinant form of BACE1 (β-site amyloid precursor protein cleaving enzyme-1) corresponding to positions 46-454 of the extracellular domain of the original membrane enzyme was prepared. The recombinant BACE1 (rBACE1) had the kinetic parameters K(m)=5.5μM and k(cat)=1719s(-1). Using several libraries
J S Nishimura et al.
The Journal of biological chemistry, 268(18), 13717-13722 (1993-06-25)
Mutant forms of Escherichia coli succinyl-CoA synthetase, W76F (Trp beta 76 replaced by Phe) (Nishimura, J. S., Mann, C. J., Ybarra, J., Mitchell, T., and Horowitz, P. M. (1990) Biochemistry 29, 862-865), and W43,76,248F (all three Trp replaced by Phe)
The activity of Clostridium histolyticum proteinase on synthetic substrates.
J D OLGE et al.
Archives of biochemistry and biophysics, 42(2), 327-336 (1953-02-01)
Caroline M S Ekblad et al.
Protein science : a publication of the Protein Society, 13(3), 617-625 (2004-02-24)
53BP1 interacts with the DNA-binding core domain of the tumor suppressor p53 and enhances p53-mediated transcriptional activation. The p53-binding region of 53BP1 maps to the C-terminal BRCT domains, which are homologous to those found in the breast cancer protein BRCA1
Sadao Manabe et al.
Microbiology (Reading, England), 156(Pt 2), 561-569 (2009-10-24)
Clostridium perfringens produces a homologue of clostripain (Clo), the arginine-specific endopeptidase of Clostridium histolyticum. To determine the biochemical and biological properties of the C. perfringens homologue (Clp), it was purified from the culture supernatant of a recombinant C. perfringens strain
Jarosław Jóźwiak et al.
FEMS immunology and medical microbiology, 45(2), 137-142 (2005-07-30)
Clostridium histolyticum culture supernatant contains numerous enzymes, which exert a cytotoxic effect on host cells. This includes lethal toxin, clostripain and high-potassium-sensitive toxin. Since the number of C. histolyticum infections increased during the last several years, it seems worthwhile to
Aprotim Mazumder et al.
Biophysical journal, 95(6), 3028-3035 (2008-06-17)
Genome organization within the cell nucleus is a result of chromatin condensation achieved by histone tail-tail interactions and other nuclear proteins that counter the outward entropic pressure of the polymeric DNA. We probed the entropic swelling of chromatin driven by
Barney Yoo et al.
Journal of the American Chemical Society, 127(49), 17132-17133 (2005-12-08)
We demonstrate that proteases can catalyze the ligation of peptidomimetic oligomers. The enzyme clostripain was used to facilitate the native ligation of N-substituted glycine oligomers, or peptoids. In addition to mediating the efficient condensation of two peptoid fragments, iterative ligation
Nicholas J Carruthers et al.
European journal of pharmacology, 555(2-3), 106-114 (2006-12-05)
Calcineurin, the Ca2+/calmodulin-dependant serine/threonine phosphatase is the target for the immunosuppressant drugs FK506 and cyclosporine-A. These established calcineurin inhibitors each require an immunophilin protein cofactor. Gossypol, a polyphenol produced by the cotton plant, inhibits calcineurin (IC50=15 microM), in a noncompetitive
Karen G Lloyd et al.
Nature, 496(7444), 215-218 (2013-03-29)
Half of the microbial cells in the Earth's oceans are found in sediments. Many of these cells are members of the Archaea, single-celled prokaryotes in a domain of life separate from Bacteria and Eukaryota. However, most of these archaea lack
Anjana Chakravorty et al.
PloS one, 6(7), e22762-e22762 (2011-08-11)
Clostridium perfringens is the causative agent of clostridial myonecrosis or gas gangrene and produces many different extracellular toxins and enzymes, including the cysteine protease α-clostripain. Mutation of the α-clostripain structural gene, ccp, alters the turnover of secreted extracellular proteins in
Asish K Bhattacharya et al.
Organic & biomolecular chemistry, 9(15), 5407-5413 (2011-05-18)
A novel one-pot route for the synthesis of benzodiazepinyl phosphonates (BDPs) has been achieved. FeCl(3) efficiently catalyzed four-component condensation of diamines, acetone and phosphites in the presence of molecular sieves to furnish BDPs as novel chemical entities with good yield.
K Guzik et al.
Cell death and differentiation, 14(1), 171-182 (2006-04-22)
The recognition of phosphatidylserine (PS) on the surface of any apoptotic cell is considered to be a key event for its clearance. We challenge this concept by showing that pretreatment of neutrophils with either host or bacterial protease affects their
Synthesis of neo-peptidoglycans: an unexpected activity of proteases.
Nicole Wehofsky et al.
Angewandte Chemie (International ed. in English), 41(15), 2735-2738 (2002-08-31)
all-D-Polypeptides: novel targets for semisynthesis.
Nicole Wehofsky et al.
Angewandte Chemie (International ed. in English), 42(6), 677-679 (2003-02-08)
Cleavage at arginine residues by clostripain.
W M Mitchell
Methods in enzymology, 47, 165-170 (1977-01-01)
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