Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:4.2.2.10 (PNL)
 341 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The ability of prenatal cerebral tissue to bind different lectins was analyzed using cryostat sections of mouse brains. It was shown that the immature cells within the embryonic cell layers possess receptors for different lectins in varying amounts. Of all lectins tested, only PNL, RCL and LPL were bound on the outer cell membranes to a considerable degree. Although the labeling patterns of PNL and RCL are similar, the latter is additionally well detectable on the wall of cerebral blood vessels. Cells of the ventricular layer are moderately labeled by PNL, which recognizes beta-D-galactosyl (1-3)-N-acetyl-D-galactosamine, but heavily labeled by LPL which binds to terminal sialic acid residues. Cells of the intermediate layer, on the other hand, are heavily stained PNL and only faintly by LPL. Hence it is suggested that the process of migration might be correlated to the removal of terminal sialic acid moieties from cell surface glycoconjugates, resulting in an exposure of the penultimate galactosyl residues.
 ...
PMID:Varying expressions of lectin receptors within embryonic cell layers of murine cerebral cortex. 719 28

Peanut (Arachis hypogaea) lectin (PNL) has been shown to agglutinate the 90% of cells from murine thymus which are supposed to be immature cortical thymocytes. Further studies on the numbers of thymocytes binding fluorescein isothiocyanate conjugated PNL (FITC-PNL) confirmed the large proportion of PNL binding cells. In other organs such as bone marrow, spleen and peripheral lymph nodes, smaller proportions of PNL positive cells have been recorded. PNL-positive cells outside the thymus have been reported to be either Thy 1-positive or null cells. It has also been suggested that PNL binding may be a marker for immaturity not only in relation to T lymphocytes but also amongst haematopoietic stem cells. Thus PNL binding as an aspect of lymphocyte differentiation is a matter of considerable interest. The current study describes the distribution of horseradish peroxidase-conjugated PNL (HRP-PNL) on frozen sections of mouse lymphoid organs. It seems that PNL binds to cells in germinal centres but not to those in some other areas containing activated lymphocytes. There is good correlation between the presence of PNL-binding germinal centres in frozen sections of lymphoid organs and the number of PNL-binding cells counted in cell suspensions from the same organs.
 ...
PMID:Peanut lectin binding properties of germinal centres of mouse lymphoid tissue. 736 Feb 73

Three extracellular pectinases were produced by Aspergillus niger CH4 by submerged and solid-state fermentation, and their physicochemical and kinetic properties were studied. The highest productivities of endo- and exo-pectinase and pectin lyase were obtained with solid-state fermentation. The kinetic and physicochemical properties of these enzymes were influenced by the type of culture method used. All activities were very different in terms of pH and temperature optima, stability at different pH and temperature values and affinity for the substrate (Km values). In solid-state fermentation, all pectinase activities were more stable at extreme pH and temperature values but the Km values of endo-pectinase and pectin lyase were higher with respect to those activities obtained by the submerged-culture technique. The pectin lyase activity obtained by the submerged-culture technique showed substrate inhibition but the enzyme obtained by solid-state fermentation did not. Electrophoresis, using sodium dodecyl sulphate/polyacrylamide gel with enzymatic extracts obtained for both culture methods, showed the same number of protein bands but some differences were found in their electrophoretic position. The results obtained in this work suggest that the culture method (submerged or solid-state) may be responsible for inducing changes in some of the pectinolytic enzymes produced by A. niger.
 ...
PMID:Production and properties of three pectinolytic activities produced by Aspergillus niger in submerged and solid-state fermentation. 757 47

In most soft-rotting Erwinia spp., including E. carotovora subsp. carotovora strain 71 (Ecc71), production of the plant cell wall degrading enzyme pectin lyase (Pnl) is activated by DNA-damaging agents such as mitomycin C (MC). Induction of Pnl production in Ecc71 requires a functional recA gene and the rdg locus. DNA sequencing and RNA analyses revealed that the rdg locus contains two regulatory genes, rdgA and rdgB, in separate transcriptional units. There is high homology between RdgA and repressors of lambdoid phages, specially phi 80. RdgB, however, has significant homology with transcriptional activators of Mu phage. Both RdgA and RdgB are also predicted to possess helix-turn-helix motifs. By replacing the rdgB promoter with the IPTG-inducible tac promoter, we have determined that rdgB by itself can activate Pnl production in Escherichia coli. However, deletion analysis of rdg+ DNA indicated that, when driven by their native promoters, functions of both rdgA and rdgB are required for the induction of pnlA expression by MC treatment. While rdgB transcription occurs only after MC treatment, a substantial level of rdgA mRNA is detected in the absence of MC treatment. Moreover, upon induction with MC, a new rdgA mRNA species, initiated from a different start site, is produced at a high level. Thus, the two closely linked rdgA and rdgB genes, required for the regulation of Pnl production, are expressed differently in Ecc71.
 ...
PMID:Nucleotide sequence, organization and expression of rdgA and rdgB genes that regulate pectin lyase production in the plant pathogenic bacterium Erwinia carotovora subsp. carotovora in response to DNA-damaging agents. 771 60

Within eight years, since October 1985 till June 1993, we had been operating on 409 patients, who had been subjected to 500 percutaneous nephrolithotomies. In 30% per cent of all the operations we had used mechanical, electrohydraulic or ultrasound lithotripsy. Out of the total number of the patients, 7 per cent had been discharged with the residual stones, but in 5.6 per cent the ESWL or spontaneous exodus had been presumed. Serious complications we had registered at 10 patients (e.g. 2 per cent of all operations). None of them however had required an emergency nephrectomy. The authors discuss the today's position of the PNL among the other operative methods of treatment of urolithiasis.
 ...
PMID:[Percutaneous nephrolithotomy]. 771 54

Pectate lyase was purified approximately 29-fold to electrophoretic homogeneity from Pseudomonas marginalis N6301. A pectate lyase (PL; EC4.2.2.2) gene of the strain was cloned and expressed in Escherichia coli. The nucleotides of the PL gene (pel) were sequenced. An open reading frame that encodes a polypeptide (molecular weight: 40,812) composed of 380 amino acids including a 29 amino acid signal peptide was assigned. The structural gene of pel consisted of 1140 base pairs. The nucleotide sequence of the 5'-flanking region of pel showed a consensus sequence of the promoter region of the pectin lyase gene (pnl) in P. marginalis N6301, a Pribnow box, and a ribosome binding site as found in E. coli.
 ...
PMID:Molecular cloning and nucleotide sequence of the pectate lyase gene from Pseudomonas marginalis N6301. 776 84

We found two enzymes that solubilize pectin from protopectin, tentatively named protopectinase-N (PPase-N) and protopectinase-R (PPase-R), in a culture filtrate of Bacillus subtilis IFO 3134. These enzymes were purified to homogeneity by hydrophobic, cation exchange and size exclusion chromatographies. The molecular weights of PPase-N and PPase-R were estimated to be 43,000 and 35,000, respectively, by SDS-PAGE. Their pIs were 9.4 and 8.2, respectively. These enzymes were stable in a wide range of pH and temperature. PPase-N and -R released water-soluble pectin by transeliminative cleavage of protopectin. According to their substrate specificities and modes of action, PPase-N and PPase-R could be classified as endo-pectate transeliminase (pectate lyase; EC 4.2.2.2) and endo-pectin transeliminase (pectin lyase; EC 4.2.2.10), respectively. Both enzymes were produced in a simple medium containing defatted soybean flour and phosphates. Production of PPase-N was repressed by addition of glucose while that of PPase-R was enhanced by phosphate.
 ...
PMID:Purification, characterization, and production of two pectic transeliminases with protopectinase activity from Bacillus subtilis. 776 45

A pectin lyase defective mutant was constructed from Erwinia carotovora Er by transposon Tn5 insertion mutagenesis to analyze the promoter region of the pnl gene, which had been cloned. The promoter of pnl is between -140 and -74 upstream of the structural gene of pnl and appears not to be regulated by Lex A.
 ...
PMID:Analysis of promoter region of the pectin lyase gene from Erwinia carotovora Er. 776 49

We constructed deletion mutant clones of a pectin lyase gene, and measured their pectin lyase activities in Escherichia coli. Pectin lyase activities were detected only in a recA+ strain but not in a recA- strain of E. coli. We also cloned and sequenced recA from Pseudomonas marginalis N6301. The recA from P. marginalis N6301 can complement recA- to form recA+ in the phenotype of E. coli. Highly conserved sequences of recA are observed among E. coli, P. fluorescens, and P. marginalis. From these results, we presume that recA is required for the expression of the pectin lyase gene in P. marginalis N6301.
 ...
PMID:Expression of a pectin lyase gene in Escherichia coli from Pseudomonas marginalis N6301. 776 26

Pectinolytic enzymes of four rumen fungi have been described. Three fungal species were monocentric Neocallimastix spp. H15, JL3 and OC2, and one isolate was a polycentric strain of Orpinomyces joyonii, A4. They differed in degree of pectin degradation and utilization. Only the strain Neocallimastix sp. H15 and partially Orpinomyces joyonii A4 were able to utilize pectin to a higher extent. The most important pectinolytic activity in all these isolates represented pectin lyase (EC 4.2.2.10) and polygalacturonase (EC 3.2.1.15). Their specific activities were in the range of 100-900 and 10-450 micrograms galacturonic acid h-1 mg protein-1 for pectin lyase and polygalacturonase, respectively. Polygalacturonase, located mainly in the endocellular fraction, was inhibited by calcium ions and had the main pH optimum at pH 6.0. All strains produced pectate lyase (EC 4.2.2.2). None of the strains tested produced pectinesterase (EC 3.1.1.11).
 ...
PMID:Pectinolytic enzymes of anaerobic fungi. 776 33


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>