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Planta Med 2012; 78 - PI266
DOI: 10.1055/s-0032-1320953
DOI: 10.1055/s-0032-1320953
Mauritanicain – a new serine protease from the latex of Euphorbia mauritanica L
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).