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Substrate Specificity and Molecular Modelling of Aspartic Proteinases (Cyprosins) from Flowers of Cynara cardunculus SUBSP. flavescens CV. Cardoon

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Aspartic Proteinases

Abstract

Water extracts of dried flowers of Cynara cardunculus subsp. flavescens cv. cardoon have been traditionally used in Portugal to produce artisanal cheeses (e.g. Serpa and Serra cheeses) with ewe’s milk. The clotting activity is due to three heterodimeric aspartic proteinases (cyprosin 1, cyprosin 2 and cyprosin 3) which have been purified from flowers.1 A native Mr of around 49000 was determined for the three cyprosins by SDS-PAGE. The subunit sizes are 32.5 + 16.5, 33.5 + 16.5, and 35.5 + 13.5 kD for cyprosin 1, 2 and 3, respectively. Gel filtration chromatography indicated somewhat lower native Mrs (41–45000). The enzymes are N-glycosylated (high mannose type) and express maximum activity around pH 4.1 using a synthetic peptide as substrate.

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Cordeiro, M. et al. (1998). Substrate Specificity and Molecular Modelling of Aspartic Proteinases (Cyprosins) from Flowers of Cynara cardunculus SUBSP. flavescens CV. Cardoon. In: James, M.N.G. (eds) Aspartic Proteinases. Advances in Experimental Medicine and Biology, vol 436. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5373-1_65

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  • DOI: https://doi.org/10.1007/978-1-4615-5373-1_65

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-7452-7

  • Online ISBN: 978-1-4615-5373-1

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