Abstract
Canine plasminogen is made up of seven domains. In each domain there are several cysteines that are linked by disulfide bonds. Reduction of a limited number of the cystines destabilizes the protein such that it precipitates. The bond or bonds that are broken provide about 14 kcal of stabilization energy. Circular dichroism and dynamic light scattering indicate that there is probably an intermediate that is formed prior to precipitation and that the intermediate is somewhat larger than the compact form of plasminogen.
Highlights
Plasminogen is a blood protein with multiple roles. It binds to many different chemical species; once bound, it can be activated via proteolysis to plasmin [1,2]
Plasminogen is thought to play a key role in the tissue remodeling that occurs during pregnancy [6,7] and that which occurs during the metastasis of tumors [8,9]
Plasminogen is thought to help in the propagation of bacterial infections [10,11,12] as well as diseases associated with prions [13,14,15]
Summary
Plasminogen (accession number P00747) is a blood protein with multiple roles. It binds to many different chemical species; once bound, it can be activated via proteolysis to plasmin [1,2]. Canine plasminogen (DPGN), the protein used in this work, consists of 793 residues which include 24 disulfide bridged cystines (48 cysteines) [23]. Blood proteins frequently contain disulfide bonds which result from the oxidation of cysteine residues that are closely positioned in the three dimensional structure.
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