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- aggregation classification "A1".
- aggregation creator B58247.
- aggregation creator person.
- aggregation creator person.
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- aggregation creator person.
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- aggregation date "1991".
- aggregation format "application/pdf".
- aggregation hasFormat 221548.bibtex.
- aggregation hasFormat 221548.csv.
- aggregation hasFormat 221548.dc.
- aggregation hasFormat 221548.didl.
- aggregation hasFormat 221548.doc.
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- aggregation isPartOf urn:issn:0014-2956.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "Production and purification of recombinant human interleukin-6 secreted by the yeast Saccharomyces cerevisiae".
- aggregation abstract "The coding region of the human interleukin-6 (hIL6) gene was fused to the prepro secretion signal of the alpha-mating factor gene in several yeast host strains. It was found that the KEX-2 protease was unable to cleave the prepro-Lys-Arg-Pro-IL6 sequence, but that unspecific cleavage of the precursor protein had occurred. The prepro-Lys-Arg-Ala-Pro-IL6 sequence, however, was correctly recognized and cleaved by the KEX-2 protease, and IL6 was efficiently secreted into the culture medium. The N-terminal Ala-Pro peptide was removed during processing by wild-type yeast strains, but was retained in a ste13 mutant. IL6 as well as the aberrant proteins were not glycosylated. The transformed cells could secrete up to 30-mu-g/ml IL6. The protein was purified from the medium to homogeneity by ion-exchange chromatography and gel filtration, and had a specific activity of about 2 x 10(8) IU/mg in a proliferation assay.".
- aggregation authorList BK147537.
- aggregation endPage "222".
- aggregation issue "1".
- aggregation startPage "217".
- aggregation volume "198".
- aggregation aggregates 619033.
- aggregation isDescribedBy 221548.
- aggregation similarTo LU-221548.