The Distribution of Estrone Sulphatase, Dehydroepiandrosterone Sulphatase, and Arylsulphatase C in the Primate (Macaca radiata) Brain and Pituitary

Abstract: Estrone sulphatase, arylsulphatase C and dehydroepiandrosterone sulphatase were measured in the pituitary, hypothalamus-preoptic area, amygdala, hippocampus, midbrain, septum, frontal cortex and occipital cortex of monkey ( Macaca radiata ) brain. All the regions showed measurable activities of all three enzymes. In all the animals tested, either the midbrain or hypothalamus-preoptic area showed the greatest activity of all three enzymes. In particular, estrone sulphatase showed the highest specific activity in either of the above two regions in all animals. Subcellular distribution studies in the hypothalamus preoptic area showed a similarity in the distribution profile between arylsulphatase C and estrone sulphatase and a significant difference of dehydroepiandrosterone sulphatase from the others.     

Interaction of antimalarial drugs with hemin

Hemin (ferriprotoporphyrin IX) is shown to form complexes with the chloroquine class of antimalarial drugs. The Soret band of hemin becomes optically active upon the addition of chiral drugs. Results on the hemin-induced quenching of the fluorescence of chloroquine are consistent with the formation of a 2:1 hemin:drug complex with a formation constant of 1.4 x 10(7) at 298 K. Also a direct comparison of the drug-treated and drug-free parasites themselves, by the noninvasive photoacoustic spectroscopic method, reveals an in vivo interaction between endogenous hemin and the added drug.     

TET2 is a component of the estrogen receptor complex and controls 5mC to 5hmC conversion at estrogen receptor cis-regulatory regions

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A novel thermostable and halostable carboxymethylcellulase from marine bacterium <Emphasis Type="Italic">Bacillus licheniformis</Emphasis>AU01

A novel thermostable, halostable carboxymethylcellulase (CMCase) from a marine bacterium Bacillus licheniformisAU01 was purified 10.4-fold with 18% yield with a specific activity of 88.43 U/mg and the molecular weight was estimated as 37 kDa. The enzyme was optimally active at pH 9–10 and temperature 50–60°C and it was most stable up to pH 12 and 20–30% of NaCl concentration. The enzyme activity was reduced when treated with Hg²⁺, Fe²⁺ and EDTA and stimulated by Co²⁺, Mn²⁺, Mg²⁺ and Ca²⁺. Various cationic, anionic detergents and commercial detergents were not much affected CMCase activity.     

Elucidation of the receptor-bound conformation of the enkephalins

The biologically relevant conformers of enkephalin predicted by solid state, solution state, and theoretical energy studies have been compared with the published structure-activity data on these compounds. No conformational technique proposes a model consistent with all the pharmacological data; the shortcomings of each approach are evaluated. An alternative approach, which correlates the structure-activity data of opiate compounds with that of the enkephalins, is described and shown to produce a model consistent with the available structure-activity data.     

Isolation of a tripeptide showing weak acetylthiocholine hydrolysing activity from a soluble form of monkey basal ganglia acetylcholinesterase by limited trypsin digestion

Acetylcholinesterase was purified from the soluble supernatant of monkey (Macaca radiata) brain basal ganglia by a three-step affinity purification procedure. The purified enzyme showed two major protein bands corresponding to molecular weights of approximately 65 kDa and approximately 58 kDa which could be labelled by [3H]diisopropylfluorophosphate. When the purified enzyme was subjected to limited trypsin digestion followed by gel filtration on Sephadex G-75 or Sephadex G-25 column, a peptide fragment of molecular weight approximately 300 Da having a weak acetylthiocholine hydrolysing activity was isolated. The amino acid sequence analysis of this peptide showed a sequence of Gly-Pro-Ser. When the [3H]DFP labelled enzyme was subjected to limited trypsin digestion and Sephadex G-75 column chromatography, a labelled peptide corresponding to approximately 430 Da was isolated. The kinetics, inhibition characteristics and binding characteristics to lectins of this peptide were compared with the parent enzyme. A synthetic peptide of sequence Gly-Pro-Ser was also found to exhibit acetylthiocholine hydrolysing activity. The kinetics and inhibition characteristics of the synthetic peptide were similar to those of the peptide derived from the purified acetylcholinesterase, except that the synthetic peptide was more specific towards acetylthiocholine than butyrylthiocholine. The specific activity (units/mg) of the synthetic peptide was about 123700 times less than that of the purified AChE.