Stephen R. Campion

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An Escherichia coli expression system that exploits the bacterial alkaline phosphatase (PhoA) signal sequence to translocate recombinant human epidermal growth factor (hEGF) to the periplasm was used to evaluate how changes in the composition and sequence of amino acids near the PhoA-hEGF junction influence the periplasmic accumulation of recombinant(More)
Three site-directed mutants of human epidermal growth factor, Leu-26----Gly, Leu-47----Ala, and Ile-23----Thr, were examined for their ability to stimulate the protein-tyrosine kinase activity of the epidermal growth factor receptor. The receptor binding affinities of the mutant growth factors were 20- to 50-fold lower, as compared to wild-type growth(More)
Improving the health of Aboriginal and Torres Strait Islander populations is the greatest challenge facing public health in Australia today. The gains in the health of the population overall have not been matched by gains among these communities. Much of the information about the health of Aboriginal and Torres Strait Islander communities and people is(More)
A synthetic chimeric gene, coding for the human epidermal growth factor fused to the signal peptide of Escherichia coli alkaline phosphatase, was cloned into E. coli under the transcriptional control of the trp-lac (tac) promoter. Following induction with isopropylthiogalactoside, the secretion of the correctly processed protein product into the bacterial(More)
In a preliminary study we demonstrated that the formation of the epidermal growth factor (EGF) receptor-ligand complex requires the participation of the highly conserved arginine 41 side chain of the growth factor peptide (Engler, D.A., Montelione, G.T., and Niyogi, S.K. (1990) FEBS Lett. 271, 47-50). In an attempt to gain further insight into the nature of(More)
This report describes the application of a simple computational tool, AAPAIR.TAB, for the systematic analysis of the cysteine-rich EGF, Sushi, and Laminin motif/sequence families at the two-amino acid level. Automated dipeptide frequency/bias analysis detects preferences in the distribution of amino acids in established protein families, by determining(More)
Eight analogues of human epidermal growth factor (hEGF) having specific amino acid substitutions in the beta-sheet structure (residues 19-31) of the amino-terminal domain were generated by site-directed mutagenesis. Affinity of the epidermal growth factor (EGF) receptor for each of these mutant hEGF analogues was measured by both radioreceptor competition(More)
Using site-directed mutagenesis, it was previously found that mutation of the individual residues Tyr13, Tyr22, Ile23, or Leu26 in the amino-terminal domain or of the highly conserved Leu47 in the carboxyl-terminal domain of human epidermal growth factor (hEGF), resulted in significantly decreased receptor binding affinity. In the present study, the(More)
The highly conserved asparagine residue at position 32 (Asn32) in the 'hinge' region of epidermal growth factor (EGF) separates the N- and C-terminal structural motifs of the EGF molecule and is therefore an appropriate target for structure-function studies. Analogs of human EGF (hEGF) were generated in which Asn32 was substituted with aspartate, glycine,(More)