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New Insights on Plasmin Long Term Stability and the Mechanism of Its Activity Inhibition Analyzed by Quartz Crystal Microbalance.

ABSTRACT: We used the research quartz crystal microbalance (RQCM) to monitor regulatory effects of plasmin and trypsin in the presence of their inhibitor α2-antiplasmin. The gold surface of quartz crystals was modified with a β-casein layer that served as a substrate for protease digestion. The addition of plasmin or trypsin as well as their mixtures with α2-antiplasmin resulted in an increase of resonant frequency, f, and in a decrease of motional resistance, Rm, depending on the molar ratio of protease: antiplasmin. At equimolar concentrations of protease and α2-antiplasmin (5 nM:5 nM) full inhibition of protease activity took place. Monitoring of plasmin activity on an hourly and daily basis revealed a prominent effect of autolysis and decrease of plasmin activity in freshly activated samples. The degree of inhibition as well as plasmin half-life (t1/2 = 2.48 ± 0.28 days) connected with its degradation was determined.

SUBMITTER: Tatarko M

PROVIDER: S-EPMC8777901 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature

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New Insights on Plasmin Long Term Stability and the Mechanism of Its Activity Inhibition Analyzed by Quartz Crystal Microbalance.

Tatarko Marek M Ivanov Ilia N IN Hianik Tibor T

Micromachines 20211229 1

We used the research quartz crystal microbalance (RQCM) to monitor regulatory effects of plasmin and trypsin in the presence of their inhibitor α2-antiplasmin. The gold surface of quartz crystals was modified with a β-casein layer that served as a substrate for protease digestion. The addition of plasmin or trypsin as well as their mixtures with α2-antiplasmin resulted in an increase of resonant frequency, f, and in a decrease of motional resistance, Rm, dependin ...[more]

PMID: 35056220

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