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- W2087842758 abstract "Recombinant pro-Der p 1 expressed in yeast Pichia pastoris was convertible into the prosequence-removed mature Der p 1 with full activities of cysteine protease and IgE-binding with or without N-glycosylation of the mature sequence as well as pro-Der f 1. The active recombinant variants will be the basis for various future studies. The major N-terminus of pro-Der p 1 with low proteolytic activity was the putative signal-cleavage site, while that of pro-Der f 1 contained not only the equivalent site but also 21 residues downstream, and pro-Der f 1 retained significant activity. Contribution of the N-terminal region of the Der p 1 prosequence including an N-glycosylation motif on effective inhibition of proteolytic activity of pro-Der p 1 was suggested." @default.
- W2087842758 created "2016-06-24" @default.
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- W2087842758 date "2002-10-09" @default.
- W2087842758 modified "2023-10-13" @default.
- W2087842758 title "Maturation of the activities of recombinant mite allergens Der p 1 and Der f 1, and its implication in the blockade of proteolytic activity" @default.
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- W2087842758 doi "https://doi.org/10.1016/s0014-5793(02)03534-2" @default.
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