Effect of Some Drugs on Sheep Liver Carbonic Anhydrase I and Ii

Abstract

Effects of clindamycin, dexketoprofen trometamol, benzylpenicillin (penicillin G) and phenoxymethylpenicillin (penicillin V) were examined on purified sheep carbonic anhydrase I and II (SCAI, SCA-II). In our study, we were chosen sheep liver tissue; because the liver is responsible for detoxification of xenobiotics. The CA isozyme have a very important duties on organisms, the effect of xenobiotics on the CA enzyme was reported. It was observed these drugs exhibited the inhibition effects against liver carbonic anhydrase isozymes I and II in our study. SCA I and SCA II isozymes were purified with about a specific activity of 1108.51 EU/mg and 5706.67 EU/mg, 120.62 and 620.96 purification fold by using Sepharose-4B-L tyrosine-sulfanilamide affinity gel chromatography. Purity of the SCA I and SCA II isozyme was checked by SDS-PAGE technique and subunit molecular masses of the SCA I was found as 29 kDa and SCA II found as 31 kDa. The usage of clindamycin, dexketoprofen trometamol, benzylpenicillin (penicillin G) and phenoxymethylpenicillin (penicillin V) in sheep liver especially during necrotic hepatitis disease is important for scientific researches. Many antibiotic and antihistamine may have dangerous effect to sheep liver. Also, it is important to study the inhibition effects of these drugs on SCA I and II isozymes.

Inhibitory effects of oxytocin and oxytocin receptor antagonist atosiban on the activities of carbonic anhydrase and acetylcholinesterase enzymes in the liver and kidney tissues of rats

“…The liver is responsible for the detoxification of xenobiotics. CA isoenzymes have very important functions in organisms, and the effects of xenobiotics on CA have been reported …”

“…CA isoenzymes have very important functions in organisms, and the effects of xenobiotics on CA have been reported. [21] J AChE) is a basic enzyme for neurotransmission, and reduces the agglomeration of active neurotransmitters in synaptic cleavage in extreme cells and hydrolyzes the neurotransmitter acetylcholine. [22] The aim of this study is to investigate the effects of OT, atosiban, which is an OT receptor antagonist, and OT-atosiban chemicals on the activities of CA and AChE enzymes in hepatic and kidney tissues of rats, which was not studied before.…”

Synthesis and In Vitro Human Carbonic Anhydrase I and II Inhibition Properties of Some Novel Hydrazone Compounds Containing an Aryl Sulfonate Moiety

“…Carbonic anhydrases (CAs, E.C.4.2.1.1), first discovered in bovine erythrocytes, are metalloenzymes containing Zn 2+ ion, which are common in all living organisms [1][2][3]. These enzymes reversibly catalyze the hydration of carbon dioxide and the dehydration of bicarbonate in living things [4][5][6].…”