Mitochondrial location of pyruvate carboxylase in Aspergillus niger

Pyruvate carboxylase has been found in the mitochondrial fraction of two strains of Aspergillus niger along with the marker enzymes of citrate synthase and cytochrome c oxidase. The location of pyruvate carboxylase in A. nidulans was, however, confirmed to be in the cytosolic fraction. The enzyme from the former sources was dependent upon the presence of acetyl-CoA for full activity; the enzyme from A. nidulans was unaffected by the presence or absence of acetyl-CoA.     

Thanatological behavior of a female Leopard (Panthera pardus fusca)

acta ethologica - We report an observation at Jhalana Leopard Reserve (JLR), Jaipur, India. On 16 March 2019, we saw a female walking up the mountain while calling her two, 4-month-old, male and...     

D-M-D Plasmonic Anti-Reflector for Next-Generation Thin c-Si Solar Cell Applications

Plasmonics - In this paper, focus is on the light trapping surface in crystalline silicon (c-Si) solar cells where thinner c-Si wafers are expected to be used by industry to reduce the cost of cell...     

Chemical Composition,Cytotoxic and Antibacterial Activities of Essential Oils of Cultivated Clones of Juniperus communis and Wild Juniperus Species

Needles of seven cultivated clones (C1 – C7) of Juniperus communis at lower altitude and three wild Juniperus species (J. communis, J. recurva and J. indica) at higher altitudes were investigated comparatively for their essential oils (EOs) yields, chemical composition, cytotoxic and antibacterial activities. The EOs yields varied from 0.26 to 0.56% (v/w) among samples. Sixty‐one volatile components were identified by gas chromatography‐mass spectrometry (GC/MS) and quantified using gas chromatography GC (FID) representing 82.5 – 95.7% of the total oil. Monoterpene hydrocarbons (49.1 – 82.8%) dominated in all samples (α‐pinene, limonene and sabinene as major components). Principal component analysis (PCA) of GC data revealed that wild and cultivated Juniperus species are highly distinct due to variation in chemical composition. J. communis (wild species) displayed cytotoxicity against SiHa (human cervical cancer), A549 (human lung carcinoma) and A431 (human skin carcinoma) cells (66.4 ± 2.2%, 74.4 ± 1.4% and 57.4 ± 4.0%), respectively, at 200 μg/ml. EOs exhibited better antibacterial activity against Gram‐positive bacteria than against Gram‐negative bacteria with the highest zone of inhibition against Staphylococcus aureus MTCC 96 (19.2 ± 0.7) by clone‐7. As per the conclusion of the findings, EOs of clone‐2, clone‐5 and clone‐7 can be suggested to the growers of lower altitude, as there is more possibility of uses of these EOs in food and medicinal preparations.     

Phosphorylation sensitizes microtubule-associated protein τ to Al3+-induced aggregation

In Alzheimer’s disease the microtubule-associated protein τ becomes hyperphosphorylated and aggregates into paired helical filaments (PHFs). Although the biochemical basis of the aggregation of τ into PHFs is not very clear, Al³⁺ has been suggested to play some role. Previous studies have shown that Al³⁺ alters the phosphorylation state and causes aggregation of τ in experimental animals and cultured neurons. In this study Al³⁺ inhibited phosphorylation of τ by neuronal cdc2-like kinase and dephosphorylation of phosphorylated τ by phosphatase 2B. These inhibitions are very likely due to Al³⁺-induced aggregations of various proteins present in phosphorylation/dephosphorylation assay mixtures since Al³⁺ caused aggregations of all proteins examined. Furthermore, compared to other proteins, τ displayed only an average sensitivity towards Al³⁺-induced aggregation. However upon phosphorylation, τ’s sensitivity towards Al³⁺ increased 3.5 fold. In the presence of the metal chelator EDTA, Al³⁺-induced aggregates of τ became soluble, whereas Al³⁺-induced phosphorylated τ aggregates were insoluble in the buffer containing EDTA and remained insensitive to proteolysis. Our data suggest that phosphorylation sensitizes τ to Al³⁺ and phosphorylated τ transforms irreversibly into a phosphatase and protease resistant aggregate in presence of this metal ion.     

Regulation of invertase levels in Avena stem segments by gibberellic Acid, sucrose, glucose, and fructose

Gibberellic acid and sucrose play significant roles in the increases in invertase and growth in Avena stem segments. About 80% of invertase is readily solubilized, whereas the rest is in the cell wall fraction. The levels of both types of invertase change in a similar manner in the response to gibberellic acid and sucrose treatment. The work described here was carried out with only the soluble enzyme. In response to a treatment, the level of invertase activity typically follows a pattern of increase followed by decrease; the increase in activity is approximately correlated with the active growth phase, whereas the decrease in activity is initiated when growth of the segments slows. A continuous supply of gibberellic acid retards the decline of enzyme activity. When gibberellic acid was pulsed to the segments treated with or without sucrose, the level of invertase activity increased at least twice as high in the presence of sucrose as in its absence, but the lag period is longer with sucrose present. Cycloheximide treatments effectively abolish the gibberellic acid-promoted growth, and the level of enzyme activity drops rapidly. Decay of invertase activity in response to cycloheximide treatment occurs regardless of gibberellic acid or sucrose treatment or both, and it is generally faster when the inhibitor is administered at the peak of enzyme induction than when given at its rising phase. Pulses with sucrose, glucose, fructose, or glucose + fructose elevate the level of invertase significantly with a lag of about 5 to 10 hours. The increase in invertase activity elicited by a sucrose pulse is about one-third that caused by a gibberellic acid pulse given at a comparable time during mid-phase of enzyme induction, and the lag before the enzyme activity increases is nearly twice as long for sucrose as for gibberellic acid. Moreover, the gibberellic acid pulse results in about three times more growth than the sucrose pulse. Our studies support the view that gibberellic acid, as well as substrate (sucrose) and end products (glucose and fructose), play a significant role in regulating invertase levels in Avena stem tissue, and that such regulation provides a mechanism for increasing the level of soluble saccharides needed for gibberellic acid-promoted growth.