Purification and characterization of recombinant human activin B

Charles H. Schmelzer, Louis E. Burton, Cathleen M. Tamony, Ralph H. Schwall, Anthony J. Mason, Nanette Liegeois

Research output: Contribution to journalArticle

Abstract

Recombinant human activin B has been isolated to more than 95% purity from a mammalian kidney cell line. Activin B is a covalently-linked homodimer with an apparent molecular mass of 25.9 kDa (unreduced) and 15.2 kDa (reduced) as determined by SDS-polyacrylamide-gel electrophoresis. On gel filtration in 6 M guanidine hydrochloride, activin B chromatographs with an apparent molecular mass of 11 kDa, whether reduced or not. The amino-terminal sequence of the purified protein is consistent with the expected sequence derived from the β subunit of inhibin B. The amino acid composition of the purified molecule agrees with the expected theoretical composition of the β subunit of inhibin B. Activin B has an apparent pI of 4.6 as determined by isoelectric focusing in 6 M urea and 4.7 as determined by chromatofocusing in 6 M urea. The extinction coefficient is 1.8.

Original languageEnglish (US)
Pages (from-to)135-141
Number of pages7
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume1039
Issue number2
DOIs
StatePublished - Jun 19 1990

Keywords

  • Activin A
  • Activin B
  • Growth factor
  • Protein purification

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology

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  • Cite this

    Schmelzer, C. H., Burton, L. E., Tamony, C. M., Schwall, R. H., Mason, A. J., & Liegeois, N. (1990). Purification and characterization of recombinant human activin B. Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, 1039(2), 135-141. https://doi.org/10.1016/0167-4838(90)90178-I