The β-domain of streptokinase affects several functionalities, including specific/proteolytic activity kinetics.

ABSTRACT: Streptokinase (SK) is a plasminogen activator which converts inactive plasminogen (Pg) to active plasmin (Pm), which cleaves fibrin clots. SK secreted by groups A, C, and G Streptococcus (SKA/SKC/SKG) is composed of three domains: SKα, SKβ and SKγ. Previous domain-swapping studies between SK1/SK2b-cluster variants revealed that SKβ plays a major role in the activation of human Pg. Here, we carried out domain-swapping between skcg-SK/SK2-cluster variants to determine the involvement of SKβ in several SK functionalities, including specific/proteolytic activity kinetics, fibrinogen-bound Pg activation and α₂ -antiplasmin resistance. Our results indicate that SKβ has a minor to determining role in these diverse functionalities for skcg-SK and SK2b variants, which might potentially b

SUBMITTER: Rafipour M 

PROVIDER: S-EPMC6609762 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature