A3422

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Showing 1-30 of 37 results for "A3422" within Papers

Selective isolation of multiple positively charged peptides for 2-DE-free quantitative proteomics.

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

An improved protocol for quantification of freshwater Actinobacteria by fluorescence in situ hybridization.

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

Studies on a new proteolytic enzyme from A chromobacter lyticus M497-1. I. Purification and some enzymatic properties.

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

Near real-time inhibitive assay for heavy metals using achromopeptidase

Shukor MY, et al.

Indian Journal of Biotechnology, 13, 398-403 (2014)

Achromopeptidase for lysis of anaerobic gram-positive cocci.

Ezaki T and Suzuki S

Journal of Clinical Microbiology, 16(5), 844-846 (1982)

Crystallization and preliminary crystallographic analysis of Achromobacter protease I mutants.

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

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)

Use of endoproteinase Lys-C from Lysobacter enzymogenes in protein sequence analysis.

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.

Studies on a new proteolytic enzyme from Achromobacter lyticus M497-1. II. specificity and inhibition studies of Achromobacter protease I.

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.

A proteomic approach reveals transient association of reticulocalbin-3, a novel member of the CREC family, with the precursor of subtilisin-like proprotein convertase, PACE4.

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

Isolation and characterization of a lysine-specific protease from Pseudomonas aeruginosa.

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

Primary structure and properties of ribonuclease Bm2 (RNase Bm2) from Bryopsis maxima.

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

Protein sequence analysis, cloning, and expression of flammutoxin, a pore-forming cytolysin from Flammulina velutipes. Maturation of dimeric precursor to monomeric active form by carboxyl-terminal truncation.

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

Phosphorylation of microtubule-associated protein tau by Ca2+/calmodulin-dependent protein kinase II in its tubulin binding sites.

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

High yield preparation of genomic DNA from Streptomyces.

Jasmina Nikodinovic et al.

BioTechniques, 35(5), 932-934 (2003-11-25)

Identification of a region of beta-amyloid precursor protein essential for its gelatinase A inhibitory activity.

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

Possible structure and function of the extra C-terminal sequence of pyruvate kinase from Bacillus stearothermophilus.

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

Performance of the BD GeneOhm MRSA achromopeptidase assay for real-time PCR detection of methicillin-resistant Staphylococcus aureus in nasal specimens.

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.

Probing PrPSc structure using chemical cross-linking and mass spectrometry: evidence of the proximity of Gly90 amino termini in the PrP 27-30 aggregate.

Bruce Onisko et al.

Biochemistry, 44(30), 10100-10109 (2005-07-27)

Elucidation of the structure of PrP(Sc) continues to be one of the most important and difficult challenges in prion research. This task, essential for gaining an understanding of the basis of prion infectivity, has been hampered by the insoluble, aggregated

A second lysine-specific serine protease from Lysobacter sp. strain IB-9374.

Shigeru Chohnan et al.

Journal of bacteriology, 186(15), 5093-5100 (2004-07-21)

A second lysyl endopeptidase gene (lepB) was found immediately upstream of the previously isolated lepA gene encoding a highly active lysyl endopeptidase in Lysobacter genomic DNA. The lepB gene consists of 2,034 nucleotides coding for a protein of 678 amino

Purification and characterization of perchloric acid soluble protein from rat lung.

M Matsumoto et al.

Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology, 135(2), 255-262 (2003-06-12)

We isolated a perchloric acid soluble protein from the post-mitochondria supernatant fraction of the rat lung and designated it as RLu-PSP1. The protein is soluble in 5% perchloric acid and was purified by ammonium sulfate fractionation and CM-Sephadex chromatography. The

Isolation and molecular characterization of multiresistant Staphylococcus sciuri and Staphylococcus haemolyticus associated with skin and soft-tissue infections.

Adebayo Shittu et al.

Journal of medical microbiology, 53(Pt 1), 51-55 (2003-12-10)

The isolation, molecular identification and genotyping of multiresistant Staphylococcus sciuri and Staphylococcus haemolyticus from skin and soft-tissue infections are reported. Accurate and full identification of three coagulase-negative staphylococcal isolates was achieved using PCR, while the API STAPH method failed to

Technical aspects of gel-based proteomics designed for elucidating an aryl hydrocarbon receptor complex.

Yoshinao Wada et al.

Environmental sciences : an international journal of environmental physiology and toxicology, 11(1), 25-31 (2005-03-05)

The identification of proteins by mass spectrometry has revolutionalized the basic method of identifying proteins constituting an intracellular unit or network for certain biological functions. The gel-based strategy following immunoprecipitation was applied to elucidating proteins associated with the aryl hydrocarbon

Insights into physiological traits of Bifidobacterium animalis subsp. lactis BB-12 through membrane proteome analysis.

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

Improvement of catalytic antibody activity by protease processing.

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

Cloning, nucleotide sequence, and expression of Achromobacter protease I gene.

T Ohara et al.

The Journal of biological chemistry, 264(34), 20625-20631 (1989-12-05)

Achromobacter protease I (API) is a lysine-specific serine protease which hydrolyzes specifically the lysyl peptide bond. A gene coding for API was cloned from Achromobacter lyticus M497-1. Nucleotide sequence of the cloned DNA fragment revealed that the gene coded for

Determination of protein oxidation by mass spectrometry and method transfer to quality control.

Damian Houde et al.

Journal of chromatography. A, 1123(2), 189-198 (2006-05-24)

Characterization and quantitative analysis of oxidation plays an important role in biopharmaceutical development. This study demonstrates an approach to the assessment of susceptible to oxidation methionine residues in monoclonal antibodies and recombinant proteins. A method for the determination of oxidation

The primary structure and structural characteristics of Achromobacter lyticus protease I, a lysine-specific serine protease.

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

Ultratrace liquid chromatography/mass spectrometry analysis of large peptides with post-translational modifications using narrow-bore poly(styrene-divinylbenzene) monolithic columns and extended range proteomic analysis.

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

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.

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