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Analysis of the interaction between α2-antiplasmin and plasmin(ogen)

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thesis
posted on 28.02.2017, 03:08 by Lu, Bernadine Gueh Cheng
Plasminogen is a multi-domain molecule which consists of a pan-apple domain, five kringles and a serine protease domain. Activation of plasminogen to plasmin converts the zymogen to a potent enzyme which dissolves blood clots. α2-antiplasmin is the physiological inhibitor of plasmin. In addition to the conserved serpin core, α2-antiplasmin also possesses two unique N- and C-terminal extensions. The conserved lysine residues (Lys427, Lys434, Lys441, Lys448 and Lys464) in the C-terminus are essential in mediating binding with plasmin kringle domains. Disrupting the interaction of the C-terminus to plasmin has been shown to decrease plasmin inhibition resulting in increased fibrinolysis. To better understand the interaction that occurs between α2-antiplasmin and plasmin, this thesis explored the basic biochemical and binding properties of these multi-domain molecules.

History

Principal supervisor

Paul B. Coughlin

Year of Award

2013

Department, School or Centre

Australian Centre for Blood Diseases

Campus location

Australia

Course

Doctor of Philosophy

Degree Type

DOCTORATE

Faculty

Faculty of Medicine Nursing and Health Sciences

Exports