| Literature DB >> 8462671 |
J Kataoka1, H Ago, N Habuka, M Furuno, C Masuta, M Miyano, A Koiwai.
Abstract
Two expression vectors were constructed to produce a putative mature alpha-pokeweed antiviral protein (alpha-PAP) in Escherichia coli with its NH2- and COOH-terminal extrapeptides excised. One was for its intracellular expression with a methionine at its NH2-terminal. The other was for its secretion using an ompA signal peptide. The former product was purified from the total soluble proteins of the transformant with a yield of 1.74 mg/liter and the latter had a yield of 5.55 mg/liter. Both products exhibited RNA N-glycosidase activity on wheat ribosomes and inhibitory activity to protein synthesis in a rabbit reticulocyte system.Entities:
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Year: 1993 PMID： 8462671 DOI： 10.1016/0014-5793(93)81651-f
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124