Cleavage specificity of purified recombinant hepatitis A virus 3C proteinase on natural substrates.

Hepatitis A virus (HAV) 3C proteinase expressed in Escherichia coli was purified to homogeneity, and its cleavage specificity towards various parts of the viral polyprotein was analyzed. Intermolecular cleavage of the P2-P3 domain of the HAV polyprotein gave rise to proteins 2A, 2B, 2C, 3ABC, and 3D...

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Vydáno v:	J Virol
Hlavní autoři:	Schultheiss, T, Sommergruber, W, Kusov, Y, Gauss-Müller, V
Médium:	Artigo
Jazyk:	Inglês
Vydáno:	American Society for Microbiology (ASM) 1995
Témata:	Research Article
On-line přístup:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC188776/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/7853510/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jvi.69.3.1727-1733.1995
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