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3 rezultatima
Characterization of "lettucine", a serine-like protease from Lactuca sativa leaves, as a novel enzyme for milk clotting.
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In this work we focused on the characterization of a novel plant rennet purified from lettuce leaves (Lactuca sativa L. cv Romana). The lettuce protease, lettucine, showed trypsin-like, SV8-like, and caseinolytic activities. Although the enzyme did not recognize peptides having hydrophobic amino
Identification of thaumatin-like protein and aspartyl protease as new major allergens in lettuce (Lactuca sativa).
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METHODS
Today, about 2-8% of the population of Western countries exhibits some type of food allergy whose impact ranges from localized symptoms confined to the oral mucosa to severe anaphylactic reactions. Consumed worldwide, lettuce is a Compositae family vegetable that can elicit allergic
Interaction of [(3)H] gibberellin A 1 with a sub-cellular fraction from lettuce (Lactuca sativa L.) hypocotyls : II. Stability and properties of the association.
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Radioactive 2,000 g pellets (2KP) derived from lettuce (Lactuca sativa) hypocotyl sections incubated with [(3)H]gibberellin A1 ([(3)H]GA1) were subjected to a range of treatments to test the stability of labelling. The labelled association was stable in 0.1 M buffer at pH 3 and pH 9 and also in 1 M
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