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The phyla Leguminosae contains protease inhibitors, lectins, chitinases, and glycohydrolases as major defense proteins in their seeds. Electrophoretic analysis of the seed proteins of tamarind ( Tamarindus indica L.), an agri-waste material, indicated the unusual presence of two major proteins comparable to overexpression of recombinant proteins. These proteins were identified by amino-terminal analysis to be (1) Kunitz-type trypsin inhibitor and (2) class III endochitinase (34000 Da). These two proteins were purified to apparent homogeneity by a single-step chitin bead affinity chromatography and characterized. The Kunitz inhibitor was specific toward inhibiting trypsin with a stoichiometry of 1:1. The 33000 +/- 1000 Da protein, accounting for >50% of the total seed protein, is an acidic glycoprotein exhibiting a very low endotype hydrolytic activity toward chitin derivatives. SDS-PAGE followed by densitometry of tamarind seed germination indicates the disappearance of the chitinase with the concomitant appearance of a cysteine endopeptidase. On the basis of its abundance, accumulation without any pathogenesis-related stimulus, temporal regulation, amino acid composition, and very low enzyme activity, this 34000 Da protein designated "tamarinin" physiologically serves as the major storage protein.
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PMID:Abundant class III acidic chitinase homologue in tamarind (Tamarindus indica) seed serves as the major storage protein. 1829 67

Cucumber seedlings were drought-stressed or inoculated with Pseudoperonospora cubensis. After 3 or 6 d the intercellular fluids of treated cucumber leaves were extracted and analyzed. Protein contents increased after pathogen inoculation and a 27-kD protein was found in intercellular fluids (Figs.1, 7). Both 27 kD proteins were purified from the intercellular fluids of cucumber leaves after drought stress or pathogen inoculation by SDS-PAGE and electro-elution protocol respectively (Fig.2, 3). Purified proteins from drought-stressed and P. cubensis infected seedlings were analyzed by MALDI-TOF MS and their peptide mass fingerprinting (PMF) results were obtained (Figs.4, 5). The PMF results were compared with protein database using the software Profound. The results show that the 27 kD proteins from seedlings after drought stress and after P. cubensis infection were the same protein, i.e. an acidic chitinase (Tables 1, 2; Fig.6). The activities of chitinase in the intercellular fluids of cucumber leaves after pathogen inoculation and in those drought stress were also analyzed. Results showed that both treatments induced the increase in chitinase activity (Fig.8), which indicated that chitinase may be involved in the protection of cucumber plant against both pathogen attack and water stress.
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PMID:[Intercellular 27 kD protein is a chitinase induced by water stress or Pseudoperonospora cubensis in cucumber leaves]. 1834 13

A chitinase (CHT1) and a chitosanase (CHS1) were purified from the culture supernatant of Pseudomonas sp. TKU015 with shrimp shell wastes as the sole carbon and nitrogen source. The optimized conditions of this new species strain (Gen Bank Accession Number EU103629) for the production of chitinases were found to be when the culture was shaken at 30 degrees C for 3 days in 100 mL of medium (pH 8) containing 0.5% shrimp shell powder (SSP) (w/v), 0.1% K2HPO4, and 0.05% MgSO(4).7H2O. The molecular weights of CHT1 and CHS1 determined by SDS-PAGE were approximately 68 kDa and 30 kDa, respectively. The optimum pH, optimum temperature, pH stability, and the thermal stability of CHT1 and CHS1 were pH 6, 50 degrees C, pH 5-7, <50 degrees C and pH 4, 50 degrees C, pH 3-9, <50 degrees C, respectively. CHT1 was inhibited completely by Mn2+ and Fe2+, and CHS1 was inhibited by Mn2+, Cu2+, and PMSF. CHT1 was only specific to chitin substrates, whereas the relative activity of CHS1 increased when the degree of deacetylation of soluble chitosan increased.
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PMID:Purification and characterization of chitinases and chitosanases from a new species strain Pseudomonas sp. TKU015 using shrimp shells as a substrate. 1837 19

This study investigated the presence of chitinases in Bacillus thuringiensis ssp kurstaki HD-1 (Bt) fermented broths of wastewater sludge (non-hydrolyzed and hydrolyzed); starch industry wastewater and soyameal. Chitinase activity was absent in soyameal and present in others. Chitinase demonstrated peaks at pH 4.0 and temperatures 40 and 50 degrees C with higher activity between pH 4-5 and 10-11. The chitinase band on SDS-PAGE was found to be between 36 and 45 kDa for non-hydrolyzed (NH) and hydrolyzed sludge (TH) and starch industry wastewater. The chitinase profile during fermentation showed peaks at 15 and 30 h for non-hydrolyzed and hydrolyzed sludge and 15 and 24 h for starch industry wastewater. Chitinase retained 96-99 % activity after two weeks incubation at room temperature and pH 4. Bioassays with supplementation of Bt chitinases showed 1.2 fold increase in entomotoxicity of wastewater sludge and a small increase in starch industry wastewater. This study sheds light on production of Bt chitinases in alternative media which will have a long term effect on entomotoxicity of these formulations.
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PMID:Bacillus thuringiensis fermentation of wastewater and wastewater sludge--presence and characterization of chitinases. 1861 15

The gene cloning, purification, properties, kinetics, and antifungal activity of chitinase from marine Streptomyces sp. DA11 associated with South China sponge Craniella australiensis were investigated. Alignment analysis of the amino acid sequence deduced from the cloned conserved 451 bp DNA sequence shows the chitinase belongs to ChiC type with 80% similarity to chitinase C precursor from Streptomyces peucetius. Through purification by 80% ammonium sulfate, affinity binding to chitin and diethylaminoethyl-cellulose anion-exchange chromatography, 6.15-fold total purification with a specific activity of 2.95 Umg(-1) was achieved. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) showed a molecular weight of approximately 34 kDa and antifungal activities were observed against Aspergillus niger and Candida albicans. The optimal pH, temperature, and salinity for chitinase activity were 8.0, 50 degrees C, and 45 g per thousand psu, respectively, which may contribute to special application of this marine microbe-derived chitinase compared with terrestrial chitinases. The chitinase activity was increased by Mn(2+), Cu(2+), and Mg(2+), while strongly inhibited by Fe(2+) and Ba(2+). Meanwhile, SDS, ethyleneglycoltetraacetic acid, urea, and ethylenediaminetetraacetic acid were found to have significantly inhibitory effect on chitinase activity. With colloidal chitin as substrates instead of powder chitin, higher V (max) (0.82 mg product/min.mg protein) and lower K (m) (0.019 mg/ml) values were achieved. The sponge's microbial symbiont with chitinase activity may contribute to chitin degradation and antifungal defense. To our knowledge, it was the first time to study sponge-associated microbial chitinase.
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PMID:Characterization of antifungal chitinase from marine Streptomyces sp. DA11 associated with South China Sea sponge Craniella australiensis. 1862 9

Two proteases (P1 and P2) and a chitinase (C1) were purified from the culture supernatant of Serratia ureilytica TKU013 with squid pen as the sole carbon/nitrogen source. The molecular masses of P1, P2 and C1 determined by SDS-PAGE were approximately 50 kDa, 50 kDa and 60 kDa, respectively. The optimum pH, optimum temperature, pH stability, and thermal stability of P1, P2 and C1 were (pH 10, 40 degrees C, pH 7-11, and <50 degrees C), (pH 10, 40 degrees C, pH 8-11, and <40 degrees C) and (pH 6, 50 degrees C, pH 5-8, and <50 degrees C), respectively. P1 and P2 were inhibited by Mg(2+), EDTA and C1 was inhibited completely by Cu(2+). The antioxidant activity of TKU013 culture supernatant was 72% per mL (DPPH scavenging ability). With this method, we have shown that squid pen wastes can be utilized and have revealed its hidden potential in the production of functional foods.
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PMID:Conversion of squid pen by Serratia ureilytica for the production of enzymes and antioxidants. 1868 16

Two extracellular chitinases were purified from Paecilomyces variotii DG-3, a chitinase producer and a nematode egg-parasitic fungus, to homogeneity by DEAE Sephadex A-50 and Sephadex G-100 chromatography. The purified enzymes were a monomer with an apparent molecular mass of 32 kDa (Chi32) and 46 kDa (Chi46), respectively, and showed chitinase activity bands with 0.01% glycol chitin as a substrate after SDS-PAGE. The first 20 and 15 N-terminal amino acid sequences of Chi32 and Chi46 were determined to be Asp-Pro-Typ-Gln-Thr-Asn-Val-Val-Tyr-Thr-Gly-Gln-Asp-Phe-Val-Ser-Pro-Asp-Leu-Phe and Asp-Ala-X-X-Tyr-Arg-Ser-Val-Ala-Tyr-Phe-Val-Asn-Trp-Ala, respectively. Optimal temperature and pH of the Chi32 and Chi46 were found to be both 60 degrees C, and 2.5 and 3.0, respectively. Chi32 was almost inhibited by metal ions Ag(+) and Hg(2+) while Chi46 by Hg(2+) and Pb(2+) at a 10 mM concentration but both enzymes were enhanced by 1 mM concentration of Co(2+). On analyzing the hydrolyzates of chitin oligomers [(GlcNAc)( n ), n = 2-6)], it was considered that Chi32 degraded chitin oligomers as an exo-type chitinase while Chi46 as an endo-type chitinase.
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PMID:Purification and characterization of chitinases from Paecilomyces variotii DG-3 parasitizing on Meloidogyne incognita eggs. 1893 94

A class III chitinase cDNA (BoChi3-1) was cloned using a cDNA library from suspension-cultured bamboo ( Bambusa oldhamii ) cells and then transformed into yeast ( Pichia pastoris X-33) for expression. Two recombinant chitinases with molecular masses of 28.3 and 35.7 kDa, respectively, were purified from the yeast's culture broth to electrophoretic homogeneity using sequential ammonium sulfate fractionation, Phenyl-Sepharose hydrophobic interaction chromatography, and Con A-Sepharose chromatography steps. N-Terminal sequencing and immunoblotting revealed that both recombinant chitinases were encoded by BoChi3-1, whereas SDS-PAGE and glycoprotein staining showed that the 35.7 kDa isoform (35.7 kDa BoCHI3-1) was glycosylated and the 28.3 kDa isoform (28.3 kDa BoCHI3-1) was not. For hydrolysis of ethylene glycol chitin (EGC), the optimal pH values were 3 and 4 for 35.7 and 28.3 kDa BoCHI3-1, respectively; the optimal temperatures were 80 and 70 degrees C, and the K(m) values were 1.35 and 0.65 mg/mL. The purified 35.7 kDa BoCHI3-1 hydrolyzed EGC more efficiently than the 28.3 kDa isoform, as compared with their specific activity and activation energy. Both recombinant BoCHI3-1 isoforms showed antifungal activity against Scolecobasidium longiphorum and displayed remarkable thermal (up to 70 degrees C) and storage (up to a year at 4 degrees C) stabilities.
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PMID:Cloning and characterization of an antifungal class III chitinase from suspension-cultured bamboo ( Bambusa oldhamii ) cells. 1899 1

Extracellular enzymes produced by Beauveria bassiana, are believed to play a key role in cuticle hydrolysis. Enzyme production and pathogenicity has been found to be positively correlated. Twenty-eight isolates of B. bassiana, collected from different geographical regions and host ranges were characterized by in vitro extracellular enzyme production and SDS-PAGE techniques for discerning biochemical basis for virulence among the different isolates. In vitro analysis of extracellular enzymes like protease, amylase, caseinase, chitinase and lipase was undertaken in an attempt to understand their relevance to virulence of the isolates. The different isolates of B. bassiana were evaluated for virulence to the second instar larvae of Helicoverpa armigera in laboratory bioassays. SDS-PAGE of total intracellular soluble proteins was also studied in order to understand affinities among the different isolates of B. bassiana. The relationship between enzyme production and pathogenicity and vice versa was nearly 50%. There was a 50% relationship associated with original insect host, pathogenicity and enzyme production.
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PMID:Relationships among activities of extracellular enzyme production and virulence against Helicoverpa armigera in Beauveria bassiana. 1902 80

The chitinase producing Penicillium sp. LYG 0704 was procured from soil of the Chonnam National University crop field. The chitinase activity was detected after the first day which increased gradually and reached its maximum after 3 days of cultivation. The chitinase was purified from a culture medium by precipitation with isopropanol and column chromatography with Mono Q and Butyl-Sepharose. The molecular mass of chitinase was estimated to be 47 kDa by SDS-PAGE. Optimal pH and temperature were 5.0 and 40 degrees C, respectively. The N-terminal amino acid sequence of the enzyme was determined to be (1)AGSYRSVAYFVDWAI(15). The fully cloned gene, 1287 bp in size, encoded a single peptide of 429 amino acids. BLAST search of the chitinase gene sequence showed similarity with chitinase of Aspergillus fumigatus Af293 chitinase gene (58%) and A. fumigatus class V chitinase ChiB1 gene (56%).
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PMID:Purification and properties of a chitinase from Penicillium sp. LYG 0704. 1911 67


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