Effect of Cysteine Substitutions on the Mitogenic Activity and Stability of Recombinant Human Keratinocyte Growth Factor

作者: L.A. Bare , M. Brown , S. Goyal , D. Idler , P.E. Mansson

DOI: 10.1006/BBRC.1994.2745

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摘要: Abstract Human Keratinocyte growth factor (hKGF), a member of the FGF family factors, contains five cysteines at amino acid positions 1, 15, 40, 102, and 106. We expressed cysteine mutants hKGF in which were cumulatively replaced with alanine or serine, starting cysteine-1. Recombinant has an inherently higher mitogenic activity stability to heat than reported for glycosylated hKGF. Mitogenic is increased additional 2.6 fold by substitution cysteine-l alanine. Mutants conserved substituted position 40 more susceptible inactivation rhKGF, but showed no significant difference inactivation. Cysteine-free rhKGF demonstrating that neither nor disulfide bonds are required activity. However, cysteine-free does not bind Heparin-Sepharose unstable compared suggesting have role maintaining KGF′s structure. This information will useful development stable potent wound healing agent from

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