Purification of soluble guanylate cyclase enzyme from human platelets.
Soluble guanylate cyclase enzyme was purified from human platelets. The soluble fraction of the lysed platelets was sequentially chromatographed over DEAE-sepharose, GTP-agarose and HPLC size-exclusion columns. About 0.1 mg of purified enzyme could be obtained from 2000 ml of platelet rich plasma. The purified enzyme had the specific activity of 205 nmoles cGMP/mg/min with Mn2+ as cofactor. The enzyme eluted at the 160,000 daltons position from the size-exclusion column. Electrophoresis in the presence of sodium dodecyl sulfate under reducing conditions revealed two subunits of 83,000 and 71,000 daltons respectively.
Chhajlani
V
V
Department of Pharmacology, Umeå University, Sweden.
Axelsson
K L
KL
Ahlner
J
J
Wikberg
J E
JE
D001792:Blood Platelets / Q000201:enzymology*; D002845:Chromatography; D004591:Electrophoresis, Polyacrylamide Gel; D006162:Guanylate Cyclase / Q000302:isolation & purification*; D006801:Humans
D006162:Guanylate Cyclase