Mauritanicain - a new serine protease from the latex of Euphorbia mauritanica L
| Autor: | Matthias F. Melzig, André Domsalla, Harshadrai M. Rawel, Martin Flemmig |
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| Předmět: |
Pharmacology
chemistry.chemical_classification Alanine Serine protease Protease Stereochemistry medicine.medical_treatment Organic Chemistry Lysine Euphorbiaceae Pharmaceutical Science Biology biology.organism_classification Analytical Chemistry Amino acid Complementary and alternative medicine chemistry Biochemistry Casein Drug Discovery biology.protein medicine Molecular Medicine Institut für Ernährungswissenschaft Leucine |
| Zdroj: | Web of Science |
| Popis: | A new protease called Mauritanicain was isolated from the latex of Euphorbia mauritanica L. (Euphorbiaceae), with a high proteolytic activity against casein. The activity was only inhibited by specific serine protease inhibitors, classifying it to the serine protease family. It is stable at temperatures from 20–90°C with an optimum in activity at 55–60°C and pH 6.5–7.5. The protease with a molecular weight of about 95 kDa shows a preference to cleave its substrates (exemplarily shown for β-lactoglobulin) behind the amino acids lysine (K), leucine (L) and alanine (A). |
| Databáze: | OpenAIRE |
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