Erythrocyte membrane-bound enzymes in Mastomys natalensis during Plasmodium berghei infection.
The pattern of activity of certain membrane-associated enzymes was followed in the erythrocytes of Plasmodium berghei-infected Mastomys natalensis. Parasitized erythrocytes were separated from non-parasitized populations by percoll-density gradient centrifugation. The activity of adenylate cyclase was markedly increased while those of ATPase, acid phosphatase, beta-glucuronidase and N-acetyl-beta-D-glucosaminidase were considerably decreased in the membrane preparations of parasitized erythrocytes as compared to normal erythrocytes. There was a decrease in the activity of ATPase and an increase of adenylate cyclase in the membrane preparations of non-parasitized erythrocytes. However, other enzymes did not alter to a significant extent in non-parasitized erythrocytes. Chloroquine (in vitro) stimulated adenylate cyclase, Na+, K+-ATPase and Ca++Mg++-ATPase while acetylcholinesterase was significantly inhibited.
D015105:3',5'-Cyclic-AMP Phosphodiesterases / Q000097:blood; D000110:Acetylcholinesterase / Q000097:blood; D000118:Acetylglucosaminidase / Q000097:blood; D000135:Acid Phosphatase / Q000097:blood; D000251:Adenosine Triphosphatases / Q000097:blood; D000262:Adenylyl Cyclases / Q000097:blood; D000818:Animals; D002499:Centrifugation, Density Gradient; D002738:Chloroquine / Q000494:pharmacology; D004910:Erythrocyte Membrane / Q000201:enzymology*; D005966:Glucuronidase / Q000097:blood; D008288:Malaria / Q000201:enzymology*; D008297:Male; D009115:Muridae; D010962:Plasmodium berghei
D002738:Chloroquine; D000110:Acetylcholinesterase; D000135:Acid Phosphatase; D015105:3',5'-Cyclic-AMP Phosphodiesterases; D005966:Glucuronidase; D000118:Acetylglucosaminidase; D000251:Adenosine Triphosphatases; D000262:Adenylyl Cyclases