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• W1969172034 abstract "While seeking conditions for single crystals of human α-l-iduronidase, solutions were discovered (pH 3.0–8.5 containing calcium or zinc salts) that transform soluble α-l-iduronidase to a solid aggregate. This aggregate is a spherulite of semi-crystalline protein. The X-ray diffraction pattern and ability to bind Congo red characterize the α-l-iduronidase spherulite as `amyloid-like', in that it displays two of the characteristics of amyloidogenic proteins. In addition, α-l-iduronidase also interacts with heparin, as do some amyloid-forming proteins." @default.
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• W1969172034 date "2000-04-01" @default.
• W1969172034 modified "2023-10-01" @default.
• W1969172034 title "α-<scp>L</scp>-Iduronidase forms semi-crystalline spherulites with amyloid-like properties" @default.
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• W1969172034 doi "https://doi.org/10.1107/s090744490000007x" @default.
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