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Biomedical subjects

M Chander

Publications and source records attributed to M Chander.

At least 19 recordsLinked to original sources
PubMed2004

Biodecolourisation of some industrial dyes by white-rot fungi.

Eight white-rot fungal strains were screened for biodecolourisation of eight dyes commercially employed in various industries. Decolourisation of Poly R 478 was used as a standard to ascertain the dye-decolourisation potential of various fungi. All the fungi tested significantly decolourised Poly R 478 on solid agar medium. When tested in a nitrogen-limited broth medium, Dichomitus squalens, Irpex flavus, Phlebia spp. and Polyporus sanguineus were better industrial dye decolourisers than Phanerochaete chrysosporium.

Agar↗
PubMed2003

Privatization of veterinary services in developing countries: a review.

Increasing fiscal constraints on the government, a lackadaisical performance by public sector animal health and breeding services and pressure from donor partners have prompted the governments of various developing countries to rethink the role of the public sector in the provision of veterinary services. Various countries have started to implement, or have already implemented, privatization of some veterinary services. The results are mixed. It is established that private provision alone is not optimal, and a blend of private and public sector veterinary services is required to utilize the virtues of both. The privatization process has also begun in India. Certain state governments in India are pursuing a cost recovery approach and are encouraging private practitioners to cope with the financial constraints and to deliver broad and effective animal health and breeding services. This paper considers the global aspects of the privatization of veterinary services as well as the scenario in India, so as to gain an insight into the very complex and debatable issue of privatization of veterinary services.

Animals↗
PubMed2003

Disaster management in India: the case of livestock and poultry.

Developing countries are becoming increasingly aware of the importance of disaster management systems, and increasing efforts are being made to streamline preparedness, response and recovery mechanisms at all levels. It is well known that many developing countries, including India, are not always well-prepared to deal with disasters. A lack of well-developed disaster management plans results in a severe loss of human life, animal life and property, which could be saved if the necessary mechanisms were in place. A lot needs to be done to improve the situation, particularly in regard to livestock. This paper describes in detail, with particular reference to India, what can be done to care for animals when natural disasters occur. The authors review various types of natural disasters and their impact on livestock, and outline different preparedness, response, recovery, and mitigation strategies. The roles of different agencies, including veterinarians, are also considered.

Animals↗
PubMed2002

Biodecolourization of azo and triphenylmethane dyes by Dichomitus squalens and Phlebia spp.

Nine white-rot fungal strains were screened for biodecolourization of brilliant green, cresol red, crystal violet, congo red and orange II. Dichomitus squalens, Phlebia fascicularia and P. floridensis decolourized all of the dyes on solid agar medium and possessed better decolourization ability than Phanerochaete chrysosporium when tested in nitrogen-limited broth medium.

Azo Compounds↗
PubMed2000

Mechanism of catalysis of the cofactor-independent phosphoglycerate mutase from Bacillus stearothermophilus. Crystal structure of the complex with 2-phosphoglycerate.

The structure of the complex between the 2, 3-diphosphoglycerate-independent phosphoglycerate mutase (iPGM) from Bacillus stearothermophilus and its 3-phosphoglycerate substrate has recently been solved, and analysis of this structure allowed formulation of a mechanism for iPGM catalysis. In order to obtain further evidence for this mechanism, we have solved the structure of this iPGM complexed with 2-phosphoglycerate and two Mn(2+) ions at 1. 7-A resolution. The structure consists of two different domains connected by two loops and interacting through a network of hydrogen bonds. This structure is consistent with the proposed mechanism for iPGM catalysis, with the two main steps in catalysis being a phosphatase reaction removing the phosphate from 2- or 3-phosphoglycerate, generating an enzyme-bound phosphoserine intermediate, followed by a phosphotransferase reaction as the phosphate is transferred from the enzyme back to the glycerate moiety. The structure also allowed the assignment of the function of the two domains of the enzyme, one of which participates in the phosphatase reaction and formation of the phosphoserine enzyme intermediate, with the other involved in the phosphotransferase reaction regenerating phosphoglycerate. Significant structural similarity has also been found between the active site of the iPGM domain catalyzing the phosphatase reaction and Escherichia coli alkaline phosphatase.

Amino Acid Sequence↗
PubMed2000

Structure and mechanism of action of a novel phosphoglycerate mutase from Bacillus stearothermophilus.

Bacillus stearothermophilus phosphoglycerate mutase (PGM), which interconverts 2- and 3-phosphoglyceric acid (PGA), does not require 2,3-diphosphoglyceric acid for activity. However, this enzyme does have an absolute and specific requirement for Mn(2+) ions for catalysis. Here we report the crystal structure of this enzyme complexed with 3PGA and manganese ions to 1.9 A resolution; this is the first crystal structure of a diphosphoglycerate-independent PGM to be determined. This information, plus the location of the two bound Mn(2+) ions and the 3PGA have allowed formulation of a possible catalytic mechanism for this PGM. In this mechanism Mn(2+) ions facilitate the transfer of the substrate's phosphate group to Ser62 to form a phosphoserine intermediate. In the subsequent phosphotransferase part of the reaction, the phosphate group is transferred from Ser62 to the O2 or O3 positions of the reoriented glycerate to yield the PGA product. Site-directed mutagenesis studies were used to confirm our mechanism and the involvement of specific enzyme residues in Mn(2+) binding and catalysis.

Amino Acid Sequence↗
PubMed1999

Structural studies on a 2,3-diphosphoglycerate independent phosphoglycerate mutase from Bacillus stearothermophilus.

Phosphoglycerate mutase (PGM), an important enzyme in the glycolytic pathway, catalyzes the transfer of a phosphate group between the 2 and the 3 positions of glyceric acid. The gene coding for the 2, 3-diphosphoglycerate independent monomeric PGM from Bacillus stearothermophilus (57 kDa), whose activity is extremely pH sensitive and has an absolute and specific requirement for Mn2+, has been cloned and the enzyme overexpressed and purified to homogeneity. Circular dichroism studies showed at most only small secondary structure changes in the enzyme upon binding to Mn2+ or its 3-phosphoglycerate substrate, but thermal unfolding analyses revealed that Mn2+ but not 3-phosphoglycerate caused a large increase in the enzyme's stability. Diffraction-quality crystals of the enzyme were obtained at neutral pH in the presence of 3-phosphoglyceric acid with ammonium sulfate as the precipitating agent; these crystals diffract X rays to beyond 2.5-A resolution and belong to the orthorhombic space group C2221 with unit cell dimensions, a = 58.42, b = 206.08, c = 124.87 A, and alpha = beta = gamma = 90.0 degrees. The selenomethionyl version of the B. stearothermophilus protein has also been overexpressed, purified, and crystallized. Employing these crystals, the determination of the three-dimensional structure of this PGM by the multiwavelength anomalous dispersion method is in progress.

2,3-Diphosphoglycerate↗
PubMed1998

The enzymatic activity of phosphoglycerate mutase from gram-positive endospore-forming bacteria requires Mn2+ and is pH sensitive.

The enzymatic activity of phosphoglycerate mutase (Pgm) from three gram-positive endospore-forming bacteria (Bacillus subtilis, Clostridium perfringens, and Sporosarcina ureae) requires Mn2+ and is very sensitive to pH; at low concentrations of Mn2+, a pH change from 8 to 6 resulted in greater than 30- to 200-fold decreases in the activity of these Pgms. However, Pgm deactivation at pH 6 was reversed by shifting the enzyme to pH 7 or 8. Free Mn2+ was not directly involved in Pgm catalysis, although enzyme-bound Mn2+ may be involved. The rate of catalysis by Mn(2+)-containing Pgm was also slightly pH dependent, although the Km for 3-phosphoglyceric acid appeared to be the same at pH 6, 7, and 8. These findings suggest that Mn2+ binds to catalytically inactive Pgm and converts it to a catalytically competent form, and further, that pH influences the efficiency with which the enzyme binds Mn2+. The extreme pH sensitivity of the Mn(2+)-dependent Pgms supports a model in which this enzyme is inhibited during sporulation by acidification of the forespore, thus allowing accumulation of the spore's large depot of 3-phosphoglyceric acid. The activity of Pgm from two closely related gram-positive bacteria that do not form spores (Planococcus citreus and Staphylococcus saprophyticus) also requires Mn2+ and is pH sensitive. In contrast, the Pgm activities from two more distantly related non-endospore-forming gram-positive bacteria (Micrococcus luteus and Streptomyces coelicolor) are neither dependent on metal ions nor particularly sensitive to pH.

Bacillus subtilis↗
PubMed1994

Cloning and sequencing of the sspF (originally 0.3 kb) genes from Bacillus cereus and Bacillus megaterium.

The sspF gene (originally 0.3 kb) of Bacillus cereus and B. megaterium has been cloned and sequenced, and the predicted amino acid sequences of the gene products (SspF) compared to that of B. subtilis SspF. These proteins exhibit an average of 74% sequence identity across species, suggesting they may play some important role in either sporulation or the dormant spore.

Bacillus cereus↗