Induction of carboxymethylcellulase inMacrophomina phaseolina

Macrophomina phaseolina, the well-known jute pathogenic fungus produces very low levels of both extra- and intracellular carboxymethylcellulase even in the absence of any cellulose as carbon source in the medium. However, the production of these enzymes is greatly induced by soluble carboxymethylcellulose. The carboxymethylcellulase inM.phaseolina is repressed by glucose.     

Interaction of antitumor drugs with human erythrocyte ghost membranes and mastocytoma P815: a spin label study.

The cytotoxic and mutagenic properties of antitumor drugs such as adriamycin, acridines, diacridine, actinomycin D and Pt compounds are related to their interaction with nucleic acids and inhibition of protein synthesis. We have examined their interaction with human erythrocyte ghost membranes and murine mastocytoma cells using spin labeling techniques. These drugs induce changes in electron spin resonance of the spin labeled ghost membranes and in the mastocytoma cells. These alterations suggest that these drugs induce changes in protein conformation of the membranes. The membrane binding properties of these drugs may be important in their mechanism of action.     

Biochemical mechanism of nitrofurantoin resistance inVibrio el tor

Vibrio el tor cells contain a constitutive reductase enzyme which converts nitrofurantoin to an active principle that is responsible for the observed antibacterial activity of the drug. Acquisition of resistance of this strain towards nitrofurantoin is associated with the loss of this reductase. This enzyme is located in the periplasmic region of the nitrofurantoin-sensitive cells, and seems to play an important role in transporting the drug into the cells.     

Structural investigations of DNA-histone complexes. A spin label study.

We have prepared two acridine spin labels, 6-chloro-9-[4-(2,2,6,6-tetramethyl-1-piperidinyloxy)amino]-2-methoxyacridine (I) and 9-[4-(2,2,6,6-tetramethyl-1-piperidinyloxy)amino]-acridine (II) and have used them to study the binding of lysine-rich histone (H1) to DNA using electron spin resonance (ESR). ESR spectra of I in the presence of DNA, polydA-polydT and polydG-polydC were characteristic of highly immobilized radicals with maximum hyperfine splitting (2T11) of 59G, 62.5G and 59G respectively. However, the 2T11 values for II in the same systems were 55.5G, 55.5G and 62.5G respectively. Addition of H1 at a low P/D released ionically bound I and II from DNA. In the presence of 0.1 M NaCl, which prevents ionic binding, H1 still caused a significant release of bound II but not I from DNA. At a high P/D (with or without NaCl) H1 caused no displacement of either I or II. Our findings suggest that H1 does not affect the intercalating sites and probably binds to one of the grooves of DNA, most probably the major groove, and specifically in the A-T-rich regions.     

Ferritin as an exogenous yolk protein in snails

Summary A main yolk component in the oocytes of the pulmonate snailPlanorbarius corneus L. has been isolated and identified as the iron storage protein ferritin by its ultrastructure, iron content, immuunological properties and behaviour in disc electrophoresis. As judged from acrylamide electrophoresis data and ultrastructural observations, yolk ferritin is an exogenous protein which is synthesised in the hepatopancreas and taken up by the oocytes by endocytosis.     

Salt distribution around roots of wheat under different transpiration rates

Summary Magnitude of Na and Cl accumulation around wheat roots was studied under different transpiration conditions in a loamy sand soil salinized with sodium chloride to an electrical conductivity of 4.1 mmho/cm in the saturation extract. A significant correlation was observed between rate of water loss per unit root length and Na and Cl content of the soil closely adhering to the roots. Under high transpiration condition, maximum ion accumulation occurred in the apparent free space of roots followed by the soil closely adhering to the roots. Results indicate that salt concentration at the root surface is markedly altered under the influence of transpiration rate such that under high transpiration conditions, the plant roots may be exposed to a much higher salt concentration than that anticipated from an analysis of the bulk soil samples.Department of Soil and Water EngineeringDepartment of Soils     

Effect of sodium butyrate on mammalian cells in culture: a review.

Sodium butyrate produces reversible changes in morphology, growth rate, and enzyme activities of several mammalian cell types in culture. Some of these changes are similar to those produced by agents which increase the intracellular level of adenosine 3',5'-cyclic monophosphate (cAMP) or by analogs of cAMP. Sodium butyrate increases the intracellular level of cAMP by about two fold in neuroblastoma cells; therefore, some of the effects of sodium butyrate on these cells may in part be mediated by cAMP. Sodium butyrate appears to have properties of a good chemotherapeutic agent for neuroblastoma tumors because the treatment of neuroblastoma cells in culture causes cell death and "differentiation"; however, it is either innocuous or produces reversible morphological and biochemical alterations in other cell types.     

Refolding of sepharose-bound trypsinogen with disulfide 179 to 203 reduced and carboxymethylated

Disulfide 179 to 203 of native bovine trypsin was reduced with sodium borohydride and converted to the S-carboxymethyl derivative. The modified zymogen was attached to CNBr-activated Sepharose, and the resulting immobilized protein was used in refolding studies. The fully reduced protein was kept at 35°, at pH 8.5, under aerobic conditions, in a mixture of reduced and oxidized glutathione, until the sulfhydryl groups were reoxidized. A maximum yield of 55% was found for the regeneration of S-(carboxymethyl)₂-trypsinogen, and the activated product, S-(carboxymethyl)₂-trypsin, reacted with an active site reagent and gave the expected specific activity toward a typical trypsin substrate. Apparently, the refolding of immobilized S-(carboxymethyl)₂-trypsinogen regenerated the native structure of trypsinogen even though one of the six disulfides could no longer be formed.     

Effect of sodium butyrate on mammalian cells in culture: A review

Summary Sodium butyrate produces reversible changes in morphology, growth rate, and enzyme activities of several mammalian cell types in culture. Some of these changes are similar to those produced by agents which increase the intracellular level of adenosine 3′,5′-cyclic monophosphate (cAMP) or by analogs of cAMP. Sodium butyrate increases the intracellular level of cAMP by about two fold in neuroblastoma cells; therefore, some of the effects of sodium butyrate on these cells may in part be mediated by cAMP. Sodium butyrate appears to have properties of a good chemotherapeutic agent for neuroblastoma tumors because the treatment of neuroblastoma cells in culture causes cell death and “differentiation”; however, it is either innocuous or produces reversible morphological and biochemical alterations in other cell types.