4.6 Article

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

期刊

MICROMACHINES
卷 13, 期 1, 页码 -

出版社

MDPI
DOI: 10.3390/mi13010055

关键词

plasmin; trypsin; alpha(2)-antiplasmin; inhibition; research quartz crystal microbalance; food quality; milk

资金

  1. DOE Office of Science User Facility [CNMS2018-293]
  2. European Union's Horizon 2020 research and innovation program through the Marie Sklodowska-Curie grant [690898]
  3. Science Grant Agency VEGA [1/0419/20]

向作者/读者索取更多资源

In this study, the regulatory effects of plasmin and trypsin in the presence of their inhibitor, alpha(2)-antiplasmin, were monitored using the research quartz crystal microbalance (RQCM). The results showed that alpha(2)-antiplasmin could fully inhibit the activity of both proteases. Additionally, it was observed that autolysis and degradation decreased the activity of plasmin in freshly activated samples. The half-life of plasmin was determined to be 2.48 ± 0.28 days.
We used the research quartz crystal microbalance (RQCM) to monitor regulatory effects of plasmin and trypsin in the presence of their inhibitor alpha(2)-antiplasmin. The gold surface of quartz crystals was modified with a beta-casein layer that served as a substrate for protease digestion. The addition of plasmin or trypsin as well as their mixtures with alpha(2)-antiplasmin resulted in an increase of resonant frequency, f, and in a decrease of motional resistance, R-m, depending on the molar ratio of protease: antiplasmin. At equimolar concentrations of protease and alpha(2)-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 (t(1/2) = 2.48 & PLUSMN; 0.28 days) connected with its degradation was determined.

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