Recombinant alkaline serine protease II degrades scrapie isoform of prion protein.
An efficient Escherichia coli expression system for the production of mature-type alkaline serine protease II (mASP II) has been constructed. Complementary deoxyribonucleic acid-encoding mASP II was inserted into the inducible bacterial expression vector pGE-30. After introduction into E. coli, the plasmid was expressed by isopropyl-1-thio-beta-D-galactopyranoside, and the recombinant product was purified using a Ni-nitrilotriacetic acid column. The purified product had the expected NH2-terminal sequence and showed a scrapie isoform of prion protein-degrading activity using hamster scrapie 263K prions as a substrate.
Hui
Zhao
Z
Department of Veterinary Physiology, Faculty of Agriculture, Kagoshima University, Kagoshima 890-0065, Japan.
Minamiguchi
Kazuhisa
K
Doi
Hiroyasu
H
Kinoshita
Naoko
N
Kanouchi
Hiroaki
H
Oka
Tatsuzo
T
D000818:Animals; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D006224:Cricetinae; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D018620:PrPSc Proteins / Q000378:metabolism*; D020033:Protein Isoforms / Q000378:metabolism*; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D012697:Serine Endopeptidases / Q000235:genetics / Q000378:metabolism*
D001426:Bacterial Proteins; D018620:PrPSc Proteins; D020033:Protein Isoforms; D011994:Recombinant Proteins; D012697:Serine Endopeptidases
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