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AssigneeNederlandse Organisatie voor toegepast-natuurwetenschappelijk onderzoek TNO
InventorsJohan Hendrikus Verheijen, Jan Roeland Occo Hanemaaijer, Natascha Alexandra Van Lent, Johannes Hendrikus Nicolaas Lindeman, Mohamed Rahoef Daha, Johanna Roos
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This invention relates to the field of determining, assaying or quantifying activity of components of the complement system. More particularly, the invention relates to methods for detecting the presence or level of activity in a sample of mannan-binding-lectin associated serine proteases (MASPs) or complexes of such proteases with lectins and to detection of the particular lectins themselves. Provided is a method for determining the activity of a MASP in a sample, comprising incubating the sample with a pro-urokinase comprising at its activation site the consensus sequence Arg/Leu/Gly-Yyy-Arg/Lys-Ile/Leu/Val-Zzz-Gly-Gly cleavable by a MASP, wherein Yyy can be any amino acid and Zzz is preferably an aliphatic amino acid, and determining proteolytic activation of said pro-urokinase.
A method for determining the activity of a mannan-binding-lectin associated serine protease (MASP) in a sample, comprising incubating the sample with a pro-urokinase comprising at its activation site the consensus sequence Arg/Leu/Gly-Yyy-Arg/Lys-Ile/Leu/Val-Zzz-Gly-Gly (SEQ ID NO:1) cleavable by a MASP, wherein Yyy can be any amino acid and Zzz is an aliphatic amino acid, and determining proteolytic activation of said pro-urokinase.
A method for determining the activity of a mannan-binding-lectin associated serine protease (MASP) in a sample, comprising incubating a sample with a recombinant non-pro-urokinase pro-enzyme, wherein its activation site comprises the activation sequence Arg/Leu/Gly-Yyy-Arg/Lys, Yyy being any amino acid, which can be cleaved at said activation site by MASP to release an active enzyme;
A modified pro-urokinase comprising in its activation site the consensus sequence Arg/Leu/Gly-Yyy-Arg/Lys-Ile/Leu/Val-Zzz-Gly-Gly (SEQ ID NO:1) cleavable by a MASP, wherein Yyy can be any amino acid and Zzz is an aliphatic amino acid, wherein said activation sequence is different from the natural activation site of pro-urokinase.
Use of pro-urokinase as reporter enzyme in a functional MASP assay.
Dependencies are inferred from the claim text.