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• W2017859962 abstract "A dimeric protease designated as EuP-82 was purified from Euphorbia cf. lactea latex. Since its proteolytic activity was inhibited by a serine protease specific inhibitor (PMSF), EuP-82 was classified as a serine protease. N-glycan deglycosylation tests revealed that EuP-82 was a glycosylated protein. MALDI-TOF MS showed that EuP-82 was a homodimer, which was its active form. The optimal conditions for fibrinogenolytic activity were at pH 11 and 35 °C. EuP-82 enzyme had broad range of pH stability from 4 to 12. Moreover, the enzyme was still active in the presence of reducing agent (β-mercaptoethanol). EuP-82 was a proline-rich enzyme (about 20.69 mol%). Increased proline production can be found in higher plants in response to both biotic and abiotic stresses, high proline in the molecule of EuP-82 might stabilize its activity, structure and folding. Based on the N-terminal amino acid sequences and peptide mass fingerprint (PMF) of EuP-82, the enzyme was identified as a new serine protease. The digested products from EuP-82 cleavage of human fibrinogen were analyzed by SDS-PAGE and PMF. The results confirmed that EuP-82 could digest all subunits of human fibrinogen. EuP-82 cleaved fibrinogen with a Michaelis constant (Km) of 3.30 ± 0.26 μM; a maximal velocity (Vmax) of 400.9 ± 0.85 ng min−1; and a catalytic efficiency (Vmax/Km) of 121.5 ± 9.25 ng μM−1 min−1. EuP-82 has potential for use in medicinal treatment, for example thrombosis, since the enzyme had fibrinogenolytic activity and high stability." @default.
• W2017859962 created "2016-06-24" @default.
• W2017859962 creator A5048591648 @default.
• W2017859962 creator A5059957384 @default.
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• W2017859962 date "2015-07-01" @default.
• W2017859962 modified "2023-09-27" @default.
• W2017859962 title "Biochemical characterization of a new glycosylated protease from Euphorbia cf. lactea latex" @default.
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• W2017859962 doi "https://doi.org/10.1016/j.plaphy.2015.04.012" @default.
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