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- W2016770107 abstract "A protein with a relative molecular mass of 31 kDa was specifically extracted by EGTA from a detergent-insoluble fraction of Giardia lamblia. N-terminal sequencing showed this protein to be identical to alpha 1-giardin, a component of the ventral disc which, based on its predicted amino acid sequence, has been classified as annexin XIX. Purified alpha 1-giardin associated with multilamellar phosphatidyl serine-containing vesicles in a Ca(2+)-dependent manner, confirming that it is a functional annexin. Molecular modelling of the amino acid sequence of the giardial annexin into the X-ray structure of annexin V suggests that the Ca(2+)-binding sites, which, as in other annexins, are all located on the convex surface of the molecule, are of the low-affinity type III." @default.
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- W2016770107 date "1999-04-01" @default.
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- W2016770107 title "Functional identification of α1-giardin as an annexin of<i>Giardia lamblia</i>" @default.
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- W2016770107 doi "https://doi.org/10.1111/j.1574-6968.1999.tb13496.x" @default.
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