alpha-L-iduronidase forms semi-crystalline spherulites with amyloid-like properties.
While seeking conditions for single crystals of human alpha-L-iduronidase, solutions were discovered (pH 3.0-8.5 containing calcium or zinc salts) that transform soluble alpha-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 alpha-L-iduronidase spherulite as 'amyloid-like', in that it displays two of the characteristics of amyloidogenic proteins. In addition, alpha-L-iduronidase also interacts with heparin, as do some amyloid-forming proteins.
Ruth
L
L
Department of Biological Chemistry and Molecular Biology Institute, University California Los Angeles, Los Angeles, CA 90095, USA.
Eisenberg
D
D
Neufeld
E F
EF
D000682:Amyloid; D000818:Animals; D016466:CHO Cells; D002118:Calcium / Q000032:analysis; D006224:Cricetinae; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D007068:Iduronidase / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry; D014162:Transfection; D015032:Zinc / Q000032:analysis
D000682:Amyloid; D011994:Recombinant Proteins; D007068:Iduronidase; D015032:Zinc; D002118:Calcium