Thermo-stable nature of aromatic monoamine-dependent superoxide-generating activity of human prion-derived Cu-binding peptides.
Human prion protein has four distinct Cu-binding motifs that catalyze the generation of superoxide coupled to oxidation of phenols and amines. Here, the thermostability of the superoxide-generating prion-derived peptides was tested. Among the peptides tested, two maintained high catalytic activity even after heating and repeated freezing/thawing cycles. The biological roles for these thermostable catalysts are discussed.
Yokawa
Ken
K
Faculty and Graduate School of Environmental Engineering, The University of Kitakyushu, Kitakyushu, Japan.
Kagenishi
Tomoko
T
Kawano
Tomonori
T
D000588:Amines / Q000737:chemistry / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003300:Copper / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism*; D011328:Prions / Q000737:chemistry*; D055550:Protein Stability; D013481:Superoxides / Q000378:metabolism*; D013696:Temperature
D000588:Amines; D010455:Peptides; D011328:Prions; D013481:Superoxides; D003300:Copper