"Activated plasmin is a 2-chain plasmin molecule held together by 2 disulfide linkages, with 5 kringle domains. Introduction of elastase removes the N-terminal domain and four kringles leaving miniplasminogen. Removal of the last kringle leaves the lone proenzyme domain, microplasminogen. Cleaving micro-plasminogen produces micro-plasmin."
Ocriplasmin (microplasmin) is a molecule created from plasminogen, one of many substances involved in blood clotting and the natural management of blood clots in the human body. It is proteolytic enzyme, meaning it is an emzyme that assists in chemical reactions on proteins. Ocriplasmin is being researched for use via intravitreal injection (injection into the eye) to treat viteromacular adhesion.
W A R N I N G: see microplasmin.org for important safety information pertaining to ocriplasmin and microplasmin, which is manufactured using recombinant DNA technologies.
ocriplasmin (microplasmin) in fibrinolysis
from "Hydrolysis of polymeric fibrin by plasmin, miniplasmin, microplasmin and trypsin" by Andrianov SI, Makogonenko EM, Kudinov SA., 1992:
125I-labeled polymeric fibrin hydrolyzed with plasmin, Val442-plasmin (miniplasmin, Lys530-plasmin (microplasmin) and trypsin has been studied for radioactivity of its separate electrophoretic bands. The reaction of hydrolysis was stopped at a moment of a two-fold decrease of the fibrin clot turbidity (t1/2) at the wave length 350 nm. For plasmin, miniplasmin, microplasmin and trypsin taken in the same caseinolytic activities t1/2 was 12.4, 40.0 164.1 and 76.8 min, respectively. Differences in composition of fibrin digests taken at t1/2, are demonstrated: the content of high-molecular components of digests decreases in the order of plasmin greater than miniplasmin greater than microplasmin greater than trypsin, thus showing differences in the processes of fibrin clot structure disruption by the enzymes.