[Certain functional characteristics of enzymatic antioxidant defense in human blood plasma].
It has been shown that human blood plasma displays a low activity of superoxide dismutase, a key enzyme of antioxidative protection. This enzyme was isolated and purified from human blood plasma by using a novel procedure based on gel filtration on Ultrogels AcA-34 and AcA-44. Data from gel filtration and disc electrophoresis in the presence of sodium dodecyl sulfate and beta-mercaptoethanol suggest that the molecular mass of the enzyme decreased with time and a simultaneous change in activity. Purification of superoxide dismutase from blood plasma revealed the presence of low molecular mass peptides (1000 and 5000 Da) which inhibited the enzyme activity. A possibility was considered for superoxide dismutase transition into an active, conformationally labile state after a split-off of the inhibiting fragment under conditions of oxidative stress.
Dubinina
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D000975:Antioxidants; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008970:Molecular Weight; D010455:Peptides / Q000502:physiology; D017382:Reactive Oxygen Species; D013482:Superoxide Dismutase / Q000037:antagonists & inhibitors / Q000097:blood* / Q000737:chemistry
D000975:Antioxidants; D010455:Peptides; D017382:Reactive Oxygen Species; D013482:Superoxide Dismutase
Nekotorye osobennosti funktsionirovaniia fermentativnoĭ antioksidantnoĭ zashchity plazmy krovi cheloveka.