D Abbott-Brown

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Thrombospondin, a high molecular weight glycoprotein secreted by platelets in response to activation by thrombin, has been identified by immunofluorescence in bovine aortic endothelial cells, human foreskin fibroblasts, and human aortic smooth muscle cells. Immunofluorescence patterns were found to be similar using antisera raised to thrombospondins(More)
We produced human monoclonal antibody that demonstrated specific reactivity to the K1 capsule of Escherichia coli and the group B polysaccharide of Neisseria meningitidis. The antibody was nonreactive with several strains of K1- E. coli and other gram-negative bacteria. All E. coli K1 clinical isolates tested were reactive with the antibody. When assayed(More)
Thrombospondin (TS), a 450,000 molecular weight glycoprotein, is released from alpha-granules of thrombin-activated platelets and is secreted and incorporated into the extracellular matrix by several cell types in culture. We have examined the effects of cell density and transformation on the production of TS in cell culture. The levels of TS, per cell, in(More)
The need to develop a blood substitute is now urgent because of the increasing concern over blood-transmitted viral and bacterial pathogens. Cell-free haemoglobin solutions and human haemoglobin synthesized in Escherichia coli and Saccharomyces cerevisiae have been investigated as potential oxygen-carrying substitutes for red blood cells. But these(More)
Recombinant human hemoglobin rHb1.1 has been genetically engineered with the replacement of the wild-type valine residues at all N-termini with methionine, an Asn 108 Lys substitution on the beta globins, and a fusion of the two alpha globins with a glycine linker. When rHb1.1 was expressed in Escherichia coli, methylation of the N-terminal methionine of(More)
The NH2-terminal extension fragment (Col 1) of the pro alpha 1(I) procollagen chain selectively inhibits the translation of procollagen mRNA in a reticulocyte lysate system, whereas the reduced and alkylated fragment (AE-Col 1) and its proteolytically derived peptides inhibit the translation of all mRNAs (Hörlein, D., McPherson, J., Goh, S. H., and(More)
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