Purification and characterization of pituitary bovine somatotropin

D. C. Wood, W. J. Salsgiver, T. R. Kasser, G. W. Lange, E. Rowold, B. N. Violand, A. Johnson, R. M. Leimgruber, G. R. Parr, N. R. Siegel, N. M. Kimack, C. E. Smith, J. F. Zobel, M. Ganguli, J. R. Garbow, G. Bild, G. G. Krivi

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Bovine somatotropin (bST) has been isolated from pituitary glands and compared in a variety of chemical analyses and bioassays with somatotropin derived from recombinant Escherichia coli. Comparison of pituitary extracts and purified bST by Western blot analysis of two-dimensional gels suggested that the immunoreactive somatotropin species present in the extract were also present in the purified material, with no significant losses or degradation as a result of the purification method. NH2-terminal sequence analysis indicated the presence of equal quantities of Ala-Phe-Pro-Ala-Met-Ser-Leu-Ser- and Phe-Pro-Ala-Met-Ser-Leu-Ser- sequences. The Met-Ser-Leu-Ser-NH2-terminal sequence, a degradation product observed in NIH standard lots, was not detected. Assay of bioactivity in a bovine liver receptor-binding assay and in a female rate growth assay showed pituitary bST and recombinant methionyl-bovine somatotropin to be equipotent. Tryptic maps and sequence analysis of pituitary-derived somatotropin suggest the presence of isoaspartate derivatization at Asp128.

Original languageEnglish
Pages (from-to)14741-14747
Number of pages7
JournalJournal of Biological Chemistry
Issue number25
StatePublished - 1989


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