Serpins (serine protease inhibitors).
Serpins are a class of proteins involved in the regulation of serine and other types of proteases. In humans, the majority of serpins regulate the functions of proteases involved in the body's response to injury. This includes roles in coagulation, fibrinolysis, inflammation, wound healing, and tissue repair. Serpins have been implicated in various animal and human pathologies by the loss of a functional serpin gene through deletion or mutation, which results in a defect in functional protein. Examples of sestorically called antithrombin III) are first described. Then, protocols to determine the second-order rate constant of AT inhibition of thrombin in the absence and presence of heparin are presented. Also provided is a partial list of other serpins and their purification methods.
Bauman
Susannah J
SJ
The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina.
Whinna
Herbert C
HC
The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina.
Church
Frank C
FC
The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina.
D000990:Antithrombin III / Q000378:metabolism; D006493:Heparin / Q000494:pharmacology; D006801:Humans; D007700:Kinetics; D008722:Methods; D015842:Serine Proteinase Inhibitors; D015843:Serpins / Q000302:isolation & purification / Q000378:metabolism / Q000502:physiology; D013917:Thrombin / Q000037:antagonists & inhibitors
D015842:Serine Proteinase Inhibitors; D015843:Serpins; D000990:Antithrombin III; D006493:Heparin; D013917:Thrombin