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- W2417996824 abstract "The characterization of proteins in their native state is essential for the understanding of pathogenic isoforms. A variant of the cysteine protease inhibitor cystatin C is the major constituent of the amyloid deposited in the cerebral vasculature of patients with the Icelandic form of hereditary cerebral hemorrhage with amyloidosis (HCHWA-I) (,). In order to study the nature of the biophysical changes owing to the Leu68Gln substitution in cystatin C, we have developed a purification procedure of human cystatin C in its native state. The protein is isolated from media of stably transfected tissue culture cells using physiological conditions that preclude protein denaturation. The importance of mild purification conditions is underscored by the finding that denaturation of the wild-type and variant proteins facilitates a similar folding of both molecules, diminishing their differences in structure and biophysical properties. Following native purification conditions, variant cystatin C has a distinct structure compared to the wild-type protein." @default.
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- W2417996824 date "2005-06-24" @default.
- W2417996824 modified "2023-10-14" @default.
- W2417996824 title "Purification of Human Wild-Type or Variant Cystatin C From Conditioned Media of Transfected Cells" @default.
- W2417996824 doi "https://doi.org/10.1385/1-59259-874-9:221" @default.
- W2417996824 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15980605" @default.
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