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Showing 1-30 of 37 results for "A3422" within Papers
Aniel Sánchez et al.
Proteomics, 6(16), 4444-4455 (2006-07-13)
A method for quantitative proteomic analysis based on the selective isolation of multiply charged peptides (RH peptides) containing arginine and histidine residues is described. Two pools of proteins are digested in tandem with lysyl-endopeptidase and trypsin and the primary amino
Raju Sekar et al.
Applied and environmental microbiology, 69(5), 2928-2935 (2003-05-07)
We tested a previously described protocol for fluorescence in situ hybridization of marine bacterioplankton with horseradish peroxidase-labeled rRNA-targeted oligonucleotide probes and catalyzed reporter deposition (CARD-FISH) in plankton samples from different lakes. The fraction of Bacteria detected by CARD-FISH was significantly
Achromopeptidase for lysis of anaerobic gram-positive cocci.
Ezaki T and Suzuki S
Journal of Clinical Microbiology, 16(5), 844-846 (1982)
Akihiko Tsuji et al.
The Biochemical journal, 396(1), 51-59 (2006-01-26)
SPCs (subtilisin-like proprotein convertases) are a family of seven structurally related serine endoproteases that are involved in the proteolytic activation of proproteins. In an effort to examine the substrate protein for PACE4 (paired basic amino-acid-cleaving enzyme-4), an SPC, a potent
T Masaki et al.
Biochimica et biophysica acta, 660(1), 44-50 (1981-07-24)
Achromobacter lyticus M497-1 produces three kinds of alkaline proteases (protease I, II and III) in culture medium along with the bacteriolytic enzyme (Masaki, T., Nakamura, K., Isono, M. and Soejima, M. (1978) Agric. Biol. Chem. 42, 1443--1445). Among these three
Len Ito et al.
Acta crystallographica. Section F, Structural biology and crystallization communications, 66(Pt 11), 1531-1532 (2010-11-04)
Achromobacter protease I (API), a serine protease, shows an order of magnitude higher activity than bovine trypsin. The optimum pH of mutant enzymes with His210 replaced by Ser (H210S) and Trp169 replaced by Phe (W169F) has been shown to shift
Near real-time inhibitive assay for heavy metals using achromopeptidase
Shukor MY, et al.
Indian Journal of Biotechnology, 13, 398-403 (2014)
T Masaki et al.
Biochimica et biophysica acta, 660(1), 51-55 (1981-07-24)
The unique specificity of Achromobacter protease I for lysine residue was investigated using synthetic and natural substrates, i.e., lysine derivatives, arginine derivatives, lysine vasopressin, substance P, ACTH and insulin. The enzyme cleaved only the -Lys-X- bonds in the above substrates.
High Intraspecific Genetic Diversity of Nocardia brasiliensis, a Pathogen Responsible for Cutaneous Nocardiosis Found in France: Phylogenetic Relationships by Using sod and hsp65 Genes
Kosova-Maali D, et al.
BioMed Research International, 2018 (2018)
P A Jekel et al.
Analytical biochemistry, 134(2), 347-354 (1983-10-15)
Endoproteinase Lys-C from Lysobacter enzymogenes, which is commercially available, proved to be useful in the determination of primary structures of proteins. The enzyme preferentially cleaves at the carboxyl side of lysine residues.
Tadashi Itagaki et al.
Biological & pharmaceutical bulletin, 29(5), 875-883 (2006-05-03)
A base non-specific ribonuclease (RNase Bm2) was isolated from a green algae (Ulvophyceae, Bryopsis maxima) as a single band on SDS-PAGE, and its primary structure and enzymatic properties, including base specificity, were investigated. The amino acid sequence of RNase Bm2
Hiroshi Sakai
Journal of biochemistry, 136(4), 471-476 (2004-12-31)
The pyruvate kinases from Genus Bacillus and a few other bacteria have an extra C-terminal sequence with a phosphoenolpyruvate binding motif composed of about 110 amino acids. To elucidate the possible structure and function of this sequence, the enzyme lacking
High yield preparation of genomic DNA from Streptomyces.
Jasmina Nikodinovic et al.
BioTechniques, 35(5), 932-934 (2003-11-25)
Hideyuki Yamamoto et al.
Archives of biochemistry and biophysics, 408(2), 255-262 (2002-12-05)
The paired helical filaments (PHF) found in Alzheimer's disease (AD) brain are composed mainly of the hyperphosphorylated form of microtubule-associated protein tau (PHF-tau). It is well known that tau is a good in vitro substrate for Ca(2+)/calmodulin-dependent protein kinase II
B W Elliott et al.
The Journal of biological chemistry, 261(24), 11259-11265 (1986-08-25)
We report here a procedure which results in the purification of an extracellular protease (designated Ps-1) from Pseudomonas aeruginosa. This enzyme cleaves fibrinogen so that the modified molecules form microcrystals and large single crystals. Precise knowledge of the Ps-1 cleavage
Parul A Patel et al.
Journal of clinical microbiology, 49(6), 2266-2268 (2011-04-22)
We evaluated the BD GeneOhm MRSA achromopeptidase (ACP) assay, which incorporates a new specimen preparation approach. A total of 1,216 leftover nasal samples were tested; using culture as the gold standard, the sensitivity and specificity were 92% and 94.6%, respectively.
Toshio Tomita et al.
The Journal of biological chemistry, 279(52), 54161-54172 (2004-10-19)
Flammutoxin (FTX), a 31-kDa pore-forming cytolysin from Flammulina velutipes, is specifically expressed during the fruiting body formation. We cloned and expressed the cDNA encoding a 272-residue protein with an identical N-terminal sequence with that of FTX but failed to obtain
Shouichi Higashi et al.
The Journal of biological chemistry, 278(16), 14020-14028 (2003-02-15)
Because beta-amyloid precursor protein (APP) has the abilities both to interact with extracellular matrix and to inhibit gelatinase A activity, this molecule is assumed to play a regulatory role in the gelatinase A-catalyzed degradation of extracellular matrix. To determine a
Metagenomic analysis of an ecological wastewater treatment plant?s microbial communities and their potential to metabolize pharmaceuticals
Balcom IN, et al.
F1000Research, 5, 844-846 (2016)
Toshiaki Hosaka et al.
Bioscience, biotechnology, and biochemistry, 68(2), 293-299 (2004-02-26)
A and B subunits of the V-type Na+-ATPase from Enterococcus hirae were suggested to possess nucleotide binding sites (Murata, T. et al., J. Biochem., 132, 789-794 (2002)), although the B subunit did not have the consensus sequence for nucleotide binding.
pH dependency of the carboxyl oxygen exchange reaction catalyzed by lysyl endopeptidase and trypsin.
Dagmar Hajkova et al.
Journal of proteome research, 5(7), 1667-1673 (2006-07-11)
The pH dependency of the carboxyl oxygen exchange reaction catalyzed by lysyl endopeptidase (Lys-C) and trypsin has been studied. The reaction was quantitatively monitored by measuring the incorporation of 18O atom into the alpha-carboxyl group of N(alpha)-acetyl-L-lysine from H2(18)O solvent.
Deuk-Sik Lee et al.
Journal of agricultural and food chemistry, 50(25), 7412-7419 (2002-11-28)
To investigate the site specificity of two transglutaminases (TGases), that is, the enzymes from guinea pig liver (GTGase) and Streptoverticillium (MTGase), the acyl acceptor and donor sites in alpha-lactalbumin were determined. Alpha-lactalbumin was cross-linked in the presence of dithiothreitol by
Krzysztof Regulski et al.
PloS one, 7(2), e32301-e32301 (2012-03-03)
Peptidoglycan (PG) is the major component of Gram positive bacteria cell wall and is essential for bacterial integrity and shape. Bacteria synthesize PG hydrolases (PGHs) which are able to cleave bonds in their own PG and play major roles in
Taro Kishimoto et al.
Proteomics, 11(3), 485-489 (2011-01-27)
Protein termini play important roles in biological processes, but there have been few methods for comprehensive terminal proteomics. We have developed a new method that can identify both the amino and the carboxyl termini of proteins. The method independently uses
Takashi Niwa et al.
Journal of microbiological methods, 61(2), 251-260 (2005-02-22)
The lytic activity of labiase and achromopeptidase for bacterial DNA/RNA extraction were compared. Rapid lysis of many bacterial strains was observed with labiase followed by SDS treatment. Both labiase and achromopeptidase showed high lytic activity against bacterial strains with the
Jian Zhang et al.
Journal of chromatography. A, 1154(1-2), 295-307 (2007-04-20)
This paper describes approaches to optimize the chromatographic performance for our recently developed LC-MS platform, extended range proteomic analysis (ERPA), for comprehensive protein characterization at the ultratrace level. Large digested peptide fragments up to 10 kDa (e.g., from lysyl endopeptidase
Microbial ecosystem analysis in root canal infections refractory to endodontic treatment
Henriques LC, et al.
Journal of Endodontics, 42(8), 1239-1245 (2016)
S Tsunasawa et al.
The Journal of biological chemistry, 264(7), 3832-3839 (1989-03-05)
The complete amino acid sequence of Achromobacter lyticus protease I (EC 3.4.21.50), which specifically hydrolyzes lysyl peptide bonds, has been established. This has been achieved by sequence analysis of the reduced and S-carboxymethylated protease and of peptides obtained by enzymatic
Ofir Gilad et al.
Journal of proteomics, 75(4), 1190-1200 (2011-11-29)
Bifidobacterium animalis subsp. lactis BB-12 is a widely used probiotic strain associated with a variety of health-promoting traits. There is, however, only limited knowledge available regarding the membrane proteome and the proteins involved in oligosaccharide transport in BB-12. We applied
Kyoko Ohara et al.
Biochemical and biophysical research communications, 315(3), 612-616 (2004-02-21)
An immunoglobulin L chain (HIR) was treated with lysyl-endopeptidase. Gel filtration chromatography of the digestion mix identified a peak displaying a significantly higher specific catalytic activity than that of the original sample. The protein in the peak was 11 kDa
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