• Volume 12, Issue 1

      March 1987,   pages  1-86

    • Wingless mutation inDrosophila melanogaster

      S G Bhat P Babu

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      A temperature sensitive lethal allele of thewingless locus ofDrosophila melanogaster together with previously studied lethal and viable alleles in this locus, has been used to study some properties of this locus. These studies show the existence of two lethal phases for thewingless lesion; one during embryogenesis and another during pupation. By growing embryos with temperature sensitivewingless lesion at the permissive temperature and letting the larvae develop at non-permissive temperature, a large-scale cell death and subsequent regeneration were seen to occur in the mutant wing discs. This cell death followed by regeneration alters the normal developmental potential of the wing disc. Disc transplantation experiments show that these discs are incapable of differentiating into wing blade structures.

    • X-ray studies on crystalline complexes involving amino acids and peptides. Part XIV: Closed conformation and head-to-tail arrangement in a new crystal form of L-histidine L-aspartate monohydrate

      C G Suresh M Vijayan

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      A new form of L-histidine L-aspartate monohydrate crystallizes in space group P22 witha = 5.131(1),b = 6.881(1),c= 18.277(2) Å,β= 97.26(1)° and Z = 2. The structure has been solved by the direct methods and refined to anR value of 0.044 for 1377 observed reflections. Both the amino acid molecules in the complex assume the energetically least favourable allowed conformation with the side chains staggered between the α-amino and α-scarboxylate groups. This results in characteristic distortions in some bond angles. The unlike molecules aggregate into alternating double layers with water molecules sandwiched between the two layers in the aspartate double layer. The molecules in each layer are arranged in a head-to-tail fashion. The aggregation pattern in the complex is fundamentally similar to that in other binary complexes involving commonly occurring L amino acids, although the molecules aggregate into single layers in them. The distribution of crystallographic (and local) symmetry elements in the old form of the complex is very different from that in the new form. So is the conformation of half the histidine molecules. Yet, the basic features of molecular aggregation, particularly the nature and the orientation of head-to-tail sequences, remain the same in both the forms. This supports the thesis that the characteristic aggregation patterns observed in crystal structures represent an intrinsic property of amino acid aggregation.

    • Immunological crossreactivity of the antisera to purified hormones

      G S Murthy N R Moudgal

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      Antisera to ovine follicle stimulating hormone free of ovine lutinising hormone contamination has been obtained in monkeys. These antisera have been shown to be able to crossreact with ovine lutinising hormone. Quantitation of the binding data for ovine follicle stimulating hormone and ovine lutinising hormone show that 10–40% of the total antibody population to ovine follicle stimulating hormone can bind to ovine lutinising hormone and the affinity constant for ovine lutinising hormone is about 2–20 times lesser than for ovine follicle stimulating hormone. These binding data indicate that there are common epitopes exposed in ovine follicle stimulating hormone and ovine lutinising hormone through the α-subunit. Results are obtained which match with the above conclusions when ovine lutinising hormone antisera is analysed for ovine follicle stimulating hormone binding. These results show that the α-subunit when combined with different β-subunits will have common epitopes exposed, but would be sterically disposed differently in the two hormones.

    • Effect of heparin on wound healing

      Sandhya Tarvady V C Anguli C V Pichappa

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      Heparin with its ability to dissolve the fibrin clot exerts its major effect in the early stages of wound healing by depriving the fibroblasts of their scaffold. Heparin inhibits cross linking of collagen and accelerates its degradation. There is faulty orientation of the collagen fibrils in the heparinized wound. It may be concluded that heparin interferes with wound healing.

    • Analysis of nucleosome arrangement on satellite DNA of rat liver chromatin

      M K Thakur

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      The arrangement of nucleosomes on the nucleotide sequence of satellite DNA of Oceanian rat (Rattus rattus) has been studied. Nucleosome cores were prepared from rat liver nuclei with micrococcal nuclease, exonucleaseIII and nuclease Sl. From the total population of core DNA fragments, the satellite-containing fragments were selected by molecular cloning and the complete nucleotide sequence of these clones was determined. The data show that nucleosomes occupy a number of preferred positions on satellite DNA. These positions are strictly defined. Thus location of nucleosomes along the satellite sequence is non-random. Such finding may have important biological significance.

    • Nitrification and simultaneous denitrification byAzospirillum brasilense 12S

      B S Kundu K R Dadarwal P Tauro

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      Azospirillum brasilense, an associative diazotrophs from sorghum roots grows autotrophically on NH4+ and CaCO3. NH4+ a is also oxidized to NO2- and then denitrified. Addition of malate to the autotrophic medium enhances both NH4+ oxidation as well as NONH2- dissimilation. The incomplete nitrification linked denitrification results in a rapid loss of nitrogen from the growth medium. The bacterium also shows assimilatory NO3- and NO2- reductases and fixes nitrogen at 50 μg N/ml of NH4+ NO3- or NO2-

    • Lipoprotein-X in hyperlipemic rat serum in chronic ethanol and acetaldehyde administration

      Ramesh Chander Narinder K Kapoor Chanan Singh

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      The levels of lipoprotein-X in circulation increased with chronic administration of ethanol or acetaldehyde. A similar profile was seen in rat serum with alkaline phosphatase activity and bilirubin content. Total cholesterol, phospholipids and triglyceride contents increased followed by a decrease by progressive feeding with ethanol or acetaldehyde. The effect of acetaldehyde was more pronounced than that of ethanol.

    • A galactomannan-hydrolysing α-galactosidase from jack fruit (Artocarpus integrifolia) seed: Affinity chromatographic purification and properties

      P S Appukuttan Debkumar Basu

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      An acid α-galactosidase from the seeds of the jack fruit seed (Artocarpus integrifolia) has been purified to homogeneity by affinity chromatography on a matrix formed by cross-linking the soluble α-galactose-bearing guar seed galactomannan. The 35kDa enzyme was a homotetramer of 9.5kDa subunits. Its carbohydrate part (5.5%) was composed of galactose and arabinose. TheKm withp-nitrophenyl α-D-galactoside as substrate was 0.35 mM. TheKi values indicated inhibition by galactose, 1-O-methyl α-galactose and melibiose in the decreasing order. Among α-galactosides, the enzyme liberated galactose from melibiose, but not from raffinose or stachyose at its pH optimum (5.2). The guar seed galactomannan was however efficiently degalactosidated; limited enzyme treatment abolished the precipitability of the polysaccharide by the α-galactose-specific jack fruit seed lectin, and complete hydrolysis yielded insoluble polysaccharide. Though similar in sugar specificity and subunit assembly, α-galactosidase and the lectin coexisting in the jack fruit seed gave no indication of immunological identity.

    • Purification and characterisation of a carboxylesterase from the latex ofSynadenium grantii Hook, ‘f’

      T Govindappa L Govardhan P S Jyothy P S Veerabhadrappa

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      The latex ofSynadenium grantii was found to contain esterolytic activity. Polyacrylamide gel electrophoretic study coupled with substrate and inhibitor specificity studies revealed the presence of multiple forms of carboxylesterases and cholinesterases in the latex. One of the carboxylesterases of the latex was purified by acetone fractionation, carboxymethyl-Sephadex chromatography and Sepharose-6B gel filtration. The homogeneity of the enzyme was established by polyacrylamide gel electrophoresis, isoelectric focussing and sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The enzyme consists of a single polypeptide chain with a molecular weight of 14,000. The amino acid analysis of the purified enzyme revealed that it contained a greater number of neutral and acidic, compared to basic amino acid residues. The isoelectric pH of the enzyme was found to be 4.0. The enzyme was a glycoprotein as revealed by periodic acid Schiff-staining technique. Studies with different organophosphate and carbamate inhibitors showed that this enzyme was sensitive to organophosphates. The product inhibition studies with this enzyme showed linear competitive inhibition with acetate and linear non-competitive inhibition with 1-naphthol.

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