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lactuca serriola/protease

Krækjan er vistuð á klemmuspjaldið
GreinarKlínískar rannsóknirEinkaleyfi
3 niðurstöður

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
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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