Lanny Ballard

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Membrane cofactor protein (MCP) of the complement system is a iC3/C3b binding molecule with cofactor activity that has been identified on all human peripheral blood cells except erythrocytes. Human mononuclear and platelet MCP is dimeric with molecular weights of 68,000 and 63,000 and is expressed in three phenotypic patterns. To further determine its(More)
Human fibronectin receptor (VLA-5) alpha and beta chain probes were used to identify their mouse homologues in a thioglycollate-elicited peritoneal exudate cell cDNA library. Sequence analysis of both alpha and beta chain-related murine clones revealed approximately 90% homology to their human counterparts by both nucleotide and derived amino acid sequence(More)
We examined the expression of VLA-5, a fibronectin receptor, during human B cell development and activation. VLA-5 is a member of the integrin supergene family; VLAs are heterodimers of at least six unique alpha chains sharing a common beta chain; most are involved in cell attachment to extracellular matrix (ECM). A hypothesis of haematopoietic development(More)
Utilizing affinity chromatography, a C3-specific binding protein was isolated from 125I surface-labeled human platelets. Analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis demonstrated two bands with mean Mr of 64,000 and 53,000, characteristic variability in the relative density of the two bands in a given individual, and the presence of(More)
Membrane cofactor protein (MCP) of human complement is an iC3/C3b-binding glycoprotein with a characteristic two-band (63 kDa and 55 kDa) pattern on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Using affinity chromatography, it has been found on human mononuclear cells and platelets. MCP has been purified and shown to be a cofactor(More)
Membrane cofactor protein (MCP or gp45-70) is a recently described regulatory glycoprotein of the complement system which binds iC3 or C3b and is present on human platelets, T cells, B cells, monocytes, and mononuclear-derived cell lines. On sodium dodecyl sulfate-polyacrylamide gel electrophoresis, MCP migrates as a doublet with an Mr of the upper band of(More)
Immune adherence is the attachment of C-bearing immune complexes via the major activation fragment of the third component of C(C3b) to C3b binding membrane proteins. On primate E, the C3b-R, termed CR1, mediates immune adherence. In nonprimates, immune adherence involves platelets instead of E. However, these functional data have not been corroborated by(More)
Membrane cofactor protein (MCP; formerly termed glycoprotein 45-70 to indicate its Mr) of complement is a widely distributed iC3/C3b binding protein with co-factor activity. On human mononuclear cells and cell lines and platelets, MCP is a doublet. The two forms differ in Mr by approximately 5 k and the upper species is predominant in most individuals. To(More)
In an attempt to develop a method of teaching thought about polarity in the general chemistry laboratory, the author has considered the application of Sentence Logic to the characterization of pure substances by solubility and conductivity. Many students of general chemistry have difficulty conceptualizing polarity. Experiments which measure solubility and(More)
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