Spectrophotometric Analysis of Bovine Serum Albumin in Presence of 1-(4-Methylphenyl)-3-Phenylprop-2-En-1-Ones.

A series of chalcones was synthesized by the Claisen-Schmidt condensation and the structures of 1- (4-methylphenyl)-3-phenylprop-2-en-1-ones were established with the help of IR and NMR study, then their effect was observed on bovine serum albumin. We have found that the synthesized chalcones interacted with bovine serum albumin and produce a great effect on their presence.

Spectrophotometric analysis of bovine serum albumin in presence of some bischalcones.

We have synthesized a series of bischalcones by the Claisen-Schmidt condensation and their effect was observed on bovine serum albumin. We have found that the synthesized bischalcones interacted with bovine serum albumin irrespective of the nature and position of the substituent with a little difference.

Spectrophotometric analysis of bovine serum albumin in presence of synthesized 1-(2’-thienyl)-(substitutedphenyl)-2-propen-1-ones.

Serum albumin an important constituent of blood, involved in transportation of a number of compounds interacts with a vast array of chemically diverse ligands, including drugs by various binding sites. Chalcones, 1,3-diaryl propenones have been found to possess diverse pharmacological activities. In the present work we report binding of bovine serum albumin with some chalcones. Series of 1-(2’- thienyl)-3(substitutedphenyl)-2-propen-1-ones were synthesized by the Claisen-Schmidt condensation and their effect was observed on bovine serum albumin. It was found that the synthesized chalcones interacted with bovine serum albumin irrespective of the nature and position of the substituent.

In-vitro studies of some chalcones on acid phosphatase.

Chemicals/compounds interact with biologically significant molecules such as enzymes, proteins, receptors, nucleic acids etc. due to the presence of various reactive groups. These interactions may result in physiological changes and are also responsible for a compound to be pharmacologically/ therapeutically active. Chalcones are known to possess significant therapeutic activities such as antiinflammatory, analgesic, antimicrobial, antioxidant, anticancer, antimalarial, antiviral, antitubercular, etc. In the present work we have evaluated the effect of chalcones on the activity of acid phosphatase of two different sources.

In-vitro studies of some carbonyl derivatives on liver acid phosphatase.

For a compound to be pharmacologically/ therapeutically active interaction of the compound with biologically significant molecules exists. It may be with a protein molecule, receptor site, enzyme, nucleic acid etc. In the present work we have evaluated the effect of semicarbazones, thiosemicarbazones and hydrazones of simple aryl aldehydes on the activity of liver acid phosphatase.

Physico-chemical properties of brain cathepsin H.

Cathepsin H (EC 3.4.22.16) from cow brain, purified to approximately 1800-fold with approximately 26% activity yield, hydrolysed BANA, Leu-2-NNap, Arg-2-NNap, and Met-2-NNap maximally at pH 6.5, 6.8, 7.0 and 7.2, respectively. It was activated by sulphydryl compounds and EDTA while sulphydryl alkylators and blockers were found to inhibit the enzyme activity. Met-2-NNap was found to be the best substrate followed by Thr-2-NNap, His-2-NNap, Leu-2-NNap, Arg-2-NNap and Ala-2-NNap, respectively. The Km values for hydrolysis of various substrates viz., Met-2-NNap, Leu-2-NNap, Arg-2-NNap, Arg-NNapOMe, Thr-2-NNap, His-2-NNap, BANA, Arg-pNA and Lys-pNA were 0.128, 0.167, 0.169, 0.288, 0.428, 0.500, 0.667, 0.195 and 0.476 mM, respectively. The temperature optima for hydrolysis of BANA and Leu-2-NNap were approximately 45 degrees C and approximately 50 degrees C with activation energies of approximately 13.7 and approximately 11.0 kcal mole-1, respectively. The enzyme was fairly stable upto 50 degrees C and between pH 4.0-7.5.

Effect of some steroidal & non-steroidal anti-inflammatory drugs on purified goat brain cathepsin L.

The lysosomal cysteine proteinases have been found to be involved in various inflammatory conditions. Inhibitory effects of certain commonly used anti-inflammatory drugs were observed on lysosomal thiol proteinase cathepsin L. Of the non-steroidal anti-inflammatory drugs tested, phenylbutazone was found to be most potent inhibitor of cathepsin L activity. The half maximal inhibition was achieved at 0.6 mM concentration. The inhibition by phenylbutazone was of non-competitive type, with a ki of 1.3 x 10(-3) M. Flufenamic acid and indomethacin were also inhibitory to cathepsin L activity, giving half maximal inhibitions at 3.5 mM and 4.5 mM concentrations respectively. In contrast, cathepsin L activity was not affected at all by steroidal anti-inflammatory agents. Aspirin was also found to have no effect on cathepsin L activity whereas salicylic acid, its m- and p-analogs exhibited inhibitory effects but to a lesser degree.

Effect of some pesticides/weedicides on cathepsin B activity and lysosomal membrane.

The in vitro inhibitory effects of various weedicides and pesticides on goat brain cathepsin B and their labilizing potency on the lysosomal membrane were quantitated. Endosulfan an organochlorine insecticide inhibited the enzymic activity to approximately 50% at 7 mM concentration followed by methyl parathion, aldrin, melathion and benzene hexachloride (BHC) in that order. Among the weedicides, butachlor was found to be most inhibitory (approximately 50% activity was lost at 6 mM) followed by isoproturone (28%) and anilophos (19%). When the labilizing/stabilizing potency of all these drugs was observed on lysosomal membrane it was found that none of these was capable of stabilizing the membrane. At 40 degrees C and 1 mM drug concentration, aldrin, endosulfan, melathion and anilophos were found to be strong labilizers of the lysosomal membrane. Others like isoproturone, BHC and methyl parathion had moderate labilizing effect. The labilization potency of the drugs was temperature dependent and was less pronounced at 25 degrees C as compared to 40 degrees C.