RECOMBINANT ALKALINE SERINE PROTEASE II DEGRADES SCRAPIE ISOFORM OF PRION PROTEIN

ZHAO HUI; KAZUHISA MINAMIGUCHI; HIROYASU DOI; NAOKO KINOSHITA; HIROAKI KANOUCHI; TATSUZO OKA

doi:10.1290/0406041.1

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ZHAO HUIhttps://orcid.org/0000-0001-6320-9731,¹ KAZUHISA MINAMIGUCHI,¹ HIROYASU DOI,¹ NAOKO KINOSHITA,¹ HIROAKI KANOUCHI,¹ TATSUZO OKA^1,*

¹Department of Veterinary Physiology, Faculty of Agriculture, Kagoshima University, Kagoshima 890-006

^*To whom correspondence should be addressed at oka@vet.agri.kagoshima-u.ac.jp

Abstract

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-β-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.

Citation Download Citation

ZHAO HUI, KAZUHISA MINAMIGUCHI, HIROYASU DOI, NAOKO KINOSHITA, HIROAKI KANOUCHI, and TATSUZO OKA "RECOMBINANT ALKALINE SERINE PROTEASE II DEGRADES SCRAPIE ISOFORM OF PRION PROTEIN," In Vitro Cellular & Developmental Biology - Animal 40(8), 293-296, (1 October 2004). https://doi.org/10.1290/0406041.1

Received: 30 June 2004; Accepted: 12 October 2004; Published: 1 October 2004