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pubmed-article:8494564pubmed:abstractTextUsing the oligonucleotide directed mutagenesis, a human lymphotoxin (TNF beta) mutant gene lacking 21 N-terminal codons has been obtained. Recombinant plasmid pLT21 for expression of the mutant gene has been constructed. The mutant gene in the plasmid was placed under control of a tandem of constitutive promoters from coliphage T7. A simple procedure for isolation of recombinant protein was developed. The procedure allows to obtain the highly purified biologically active mutant protein with a good yield. During biosynthesis the recombinant protein undergoes a posttranslational processing resulted in the cleavage of N-terminal methionine and leucine residues.lld:pubmed
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pubmed-article:8494564pubmed:pagination414-9lld:pubmed
pubmed-article:8494564pubmed:dateRevised2008-11-21lld:pubmed
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pubmed-article:8494564pubmed:year1993lld:pubmed
pubmed-article:8494564pubmed:articleTitle[Preparation and bacterial expression of a mutant gene for human lymphotoxin].lld:pubmed
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pubmed-article:8494564pubmed:publicationTypeEnglish Abstractlld:pubmed