Biomedical subjects
Publications and source records attributed to J C Ford.
In trabecular bone the NMR linewidth is found to be governed by the magnetic field inhomogeneity arising from the difference in magnetic permeability between bone and marrow. T2* was measured in vivo in the distal femur by interferometry and localized spectroscopy. Both methods showed T2* to be inversely related to trabecular plate density.
A new approach to probe the structure of trabecular bone in the vertebral bodies in humans was evaluated, and preliminary data are presented. The proposed method is based on the hypothesis that the presence of two physical phases--bone and bone marrow--causes a magnetic field distribution across the imaging voxel. The resulting spread in resonance frequency produces line broadening, which is measured as the decay rate of the region of interest signal intensity that has the properties of an interferogram. The interferogram is the result of two principal chemically shifted components of bone marrow--fat and water--getting in and out of phase with one another while being attenuated by T2* processes from the magnetic field distribution within the measuring volume. The time constant for the decay (T2*) can then be obtained by means of curve-fitting techniques. T2* in healthy persons is found to increase slightly with age. However, patients with osteoporosis (low bone mineral density and/or spine compression fractures) have significantly prolonged T2* values, which are interpreted as arising from an increase in the intertrabecular space.
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Comparison of the gradient reversed-phase chromatographic retentions of twelve Staphylococcal nuclease mutants and the naturally occurring protein showed that the chain location and the chemical nature of the substituted amino acid(s) were equally significant in determining the retention. Correlations between the retention times of these nuclease mutants and of previously published data for interleukin 2 mutants and insulin variants with nineteen amino acid-based predictive scales revealed retention time to be significantly correlated to several scales. The use of mutagenized proteins allowed a more sensitive analysis of the individual amino acid contributions to retention than can be achieved by utilizing a more diverse set of proteins.
In man, the immune response genes are located within the HLA-D/DR region, and the gene products, the Ia antigens, are expressed on B lymphocytes, monocytes, and a percentage of null cells and activated T lymphocytes. We recently identified a human Ia antigen, K19, which appeared to be limited in its expression to B lymphocytes, and to be preferentially expressed on the more mature cells within this population. This work was facilitated by a monoclonal antibody. HK-19, which recognized a monomorphic determinant of this Ia molecule. We now report the characterization of a second monoclonal antibody, HK-13, which recognized the same molecule as HK-19, but only on cells from some individuals. The greater affinity of HK-13 allowed more complete characterization of the K19/K13 molecule. This characterization included cytofluorography, two-dimensional gel electrophoresis, tryptic peptide mapping, and partial N-terminal amino acid sequencing, and indicated that K19 and K13 were epitopes on HLA-DQ (DC) molecules. The pattern of reactivity of HK-13 on a panel of typing cells did not correlate with any of the known HLA-DQ polymorphic determinants. Thus, HK-13 is a new polymorphic determinant of the HLA-DQ series.