Journal article

PURIFICATION AND PROPERTIES OF BACTERIALLY SYNTHESIZED HUMAN GRANULOCYTE-MACROPHAGE COLONY STIMULATING FACTOR

AW BURGESS, CG BEGLEY, GR JOHNSON, AF LOPEZ, DJ WILLIAMSON, JJ MERMOD, RJ SIMPSON, A SCHMITZ, JF DELAMARTER

Blood | W B SAUNDERS CO | Published : 1987

Abstract

Human granulocyte-macrophage colony stimulating factor (GM-CSF) has been synthesized in high yield using a temperature inducible plasmid in Escherichia coli. The human GM-CSF is readily isolated from the bacterial proteins because of its differential solubility and chromatographic properties. The bacterially synthesized form of the human GM-CSF contains an extra methionine residue at position 1, but otherwise it is identical to the polypeptide predicted from the cDNA sequence. The specific activity of 2.9 X 10(7) units/mg of protein for purified bacterially synthesized human GM-CSF indicates that despite the lack of glycosylation, the molecule is substantially in its native conformation. Thi..

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