The existence of glutathione and cysteine disulfide-linked to erythrocyte carbonic anhydrase from tiger shark.
In this study it is shown that the higher molecular weight previously reported for tiger shark carbonic anhydrase (carbonate hydro-lyase, EC 4.2.1.1) compared to other carbonic anhydrases is decreased to a normal value around 30 000 after disulfide reduction of the enzyme. This difference in molecular weight is at least partly due to the existence of disulfide-linked glutathione and cysteine residues. Approx. 3 mol glutathione and a similar amount of cysteine are shown to be bound per mol enzyme. The presence of these factors also has effects on the enzyme activity.
Bergenhem
N
N
Carlsson
U
U
Strid
L
L
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002250:Carbon Radioisotopes; D002256:Carbonic Anhydrases / Q000097:blood* / Q000302:isolation & purification; D003545:Cysteine / Q000032:analysis*; D004912:Erythrocytes / Q000201:enzymology*; D005978:Glutathione / Q000031:analogs & derivatives* / Q000032:analysis / Q000302:isolation & purification; D019803:Glutathione Disulfide; D007461:Iodoacetates / Q000378:metabolism; D019807:Iodoacetic Acid; D008970:Molecular Weight; D012754:Sharks
D000596:Amino Acids; D002250:Carbon Radioisotopes; D007461:Iodoacetates; D002256:Carbonic Anhydrases; D005978:Glutathione; D003545:Cysteine; D019803:Glutathione Disulfide; D019807:Iodoacetic Acid