[Phospholipase A2 activity in human platelets. Isolation and purification of the enzyme].
The activity of phospholipase A2 in blood platelets of healthy donors and IHD patients was examined. The enzyme activity was found to be increased 3-fold in platelets possessing a high level of functional activity (IHD) and by one order of magnitude in patients with myocardial infarction as compared with healthy donors. An enzyme preparation possessing a phospholipase activity was isolated from platelets by using salt extraction (KCl) and sonication. Purification of the enzyme by affinity chromatography resulted in two protein peaks both having a phospholipase A2 activity, the purification and molecular masses of these fractions being 768- and 2200-fold, and 13.5 and 15 kDa, respectively. It was supposed that these proteins are substrate-specific forms of phospholipase A2.
Muratova
U Z
UZ
Bornikov
V T
VT
Abdukaiumova
A Kh
AKh
Saatov
T S
TS
D000818:Animals; D001792:Blood Platelets / Q000201:enzymology*; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008930:Mitochondria, Liver / Q000201:enzymology; D009203:Myocardial Infarction / Q000201:enzymology; D010741:Phospholipases A / Q000302:isolation & purification / Q000378:metabolism*; D054467:Phospholipases A2; D051381:Rats; D013056:Spectrophotometry, Ultraviolet; D013379:Substrate Specificity
D010741:Phospholipases A; D054467:Phospholipases A2
Aktivnost' fosfolipazy A2 v trombotsitakh cheloveka. Vydelenie i ochistka fermenta.