INTERACTION OF LIGHT QUALITY AND NUCLEASES IN THE GROWTH OF THE GAMETOPHYTES OF ASPLENIUM NIDUS

Appropriate concentrations of ribonuclease A and B selectively inhibited initiation of two-dimensional morphology in the gametophytes of Asplenium nidus, grown under a photoperiod of 5½ hr white light. Filamentous growth was promoted in such sporelings, the individual cells of which were significantly longer than corresponding cells of the control. Higher concentrations of enzymes were required to inhibit two-dimensional growth in the gametophytes grown in blue light. Concentrations of ribonuclease A or B which inhibited two-dimensional growth in white light promoted growth in length of the protonema in red light. Growth modifications in the sporelings induced by deoxyribonuclease in different light conditions were similar to those induced by the ribonucleases. The results lend further support to the postulated role of RNA in the regulation of two-dimensional growth in fern gametophytes.     

Mechanical instability of adherens junctions overrides intrinsic quiescence of hair follicle stem cells

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The identity and distribution of striped bagrid catfish,Mystus tengara (Hamilton 1822) revealed through integrative taxonomy

Molecular Biology Reports - The taxonomic status and geographical distribution of M. tengara are vague. No genetic diversity and phylogenetic study have been done till now to resolve its identity...     

Correction to: Overview on cyanobacterial exopolysaccharides and biofilms: role in bioremediation

Reviews in Environmental Science and Bio/Technology -     

Active and pro-plasminogen activator on the surface of human bladder cancer cells derived from a high grade invasive tumour

Intact UCRU-BL28 cells derived from a high grade invasive human bladder cancer produced both active and pro-plasminogen activator. Following culture of cells in the presence of plasminogen, all of the pro-plasminogen activator was converted to an active form. Cell-surface extracts showed plasminogen activator activity with a molecular mass of 55,000, similar to that of human urokinase. Extracts also contained gelatinase activities with molecular masses of 101,000; 80,000; 74,000 and 70,000 in polyacrylamide gel electrophoresis. These tumour cell-surface proteinases may be involved in invasion and metastasis in human bladder cancer.     

Adsorption of Bovine Serum Albumin from salt solution onto activated carbon

One of the wastewaters from tanning industry (soak liquor) contains 0.4 g/l of dissolved protein. During coagulation and flocculation 41 % of protein was removed. A suggestion has been made to remove the residual protein by adsorption technique. The optimum conditions for adsorption of Bovine Serum Albumin (BSA) on rice bran based activated carbon (RBAC) have been determined. Maximum adsorption of BSA took place at pH 7.O. Ionic strength was found to have influence on the adsorption behaviour. Adsorption capacity of BSA onto charcoal surface decreased with increase in temperature. Enthalpy of adsorption in all cases was found to be within –19 to –57 kJ/mole, indicating exothermic nature of the process. Applicability of adsorption technique to the removal of dissolved protein from soak water has been studied. The maximum removal of protein occurred at pH 7.0 and the ratio of protein removed to weight of adsorbent was 3.22×10^–3 g/g.     

Hydroxypyruvate-mediated regulation of oxalate synthesis by lactate dehydrogenase and its relevance to primary hyperoxaluria type II

Hydroxypyruvate (HP) brought about the decarboxylation of [1-14C] glyoxylate nonenzymically at all pH values considered. The rate of decomposition of glyoxylate increased with each increase in the concentrations of the reactants, the pH, and temperature and on the addition of the cations Fe2+, Mn2+, Mg2+, Zn2+, Co2+, and Cu2+. The addition of HP to a purified preparation of lactate dehydrogenase (LDH) catalyzing the oxidation of [1-14C]glyoxylate to [14C]oxalate in the presence of either NAD or NADH inhibited the production of oxalate. These observations have their implications in L-glyceric aciduria (primary hyperoxaluria type II), a syndrome characterized by the accumulation of HP and recurrent oxalosis. They suggest that the accumulating HP may reduce the contribution of intracellular glyoxylate to the formation of oxalate by competitively inhibiting the liver LDH. The involvement of liver LDH in oxalate synthesis and its postulated induction by HP and NAD in vivo are, therefore, reexamined.     

Hyperoxaluria in L-glyceric aciduria: possible nonenzymic mechanism

Hydroxypyruvate inhibited the oxidation of [1-14C]glyoxylate to [14C] oxalate whether catalyzed by a purified preparation of glycolic acid oxidase from human liver, lactate dehydrogenase, a human liver extract, or a lobe of rat liver. It also brought about the nonenzymic decarboxylation of [1-14C]glyoxylate when it was present in the above assay systems. Radioactive isotope dilution and high-performance liquid chromatography analysis revealed the autooxidation of hydroxypyruvate to oxalate on standing in buffered solution at pH 7.4. In view of these observations, the current hypothesis of the role of lactate dehydrogenase in inducing hyperoxaluria in L-glyceric aciduria has been reexamined, and a possible nonenzymic mechanism by which oxalate may originate from hydroxypyruvate under such conditions has been proposed.