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D Windsor

Publications and source records attributed to D Windsor.

21 records · Page 2Linked to original sources

Changes in lipoprotein metabolism and body composition in chickens in response to divergent selection for plasma very low density lipoprotein concentration.

1. Plasma lipoprotein metabolism and body composition in lines of chicken selected for high- and low-plasma very low density lipoprotein (VLDL) concentrations were compared to the commercial broiler (meat-type) line from which they were derived. 2. Selection for low-plasma VLDL concentration for 10 generations has reduced the rate of VLDL secretion by at least 50% in males whereas selection for high-VLDL concentration has increased the rate of VLDL secretion over 2-fold. 3. Body fat content was highly correlated with rate of secretion of plasma triglyceride-rich (TGR) lipoproteins (r = 0.88 over the three lines). However, extrapolation of the data suggests that birds secreting no TGR-lipoproteins into the plasma would still have substantial amounts of body fat. 4. Selection for high VLDL has increased the proportion of circulating VLDL-triglyceride taken up by the abdominal fat pad by over 2-fold but there was no difference between high- and low-VLDL lines in the proportion of VLDL-triglyceride taken up by tissues and oxidised to [14C]-carbon dioxide. 5. The results confirm the importance of plasma lipoprotein metabolism in determining body composition in the chicken but suggest there are limits to further reduction in body fat content by manipulation of plasma lipoprotein metabolism.

Adipose Tissue↗

Molecular location of a species-specific epitope on the hamster scrapie agent protein.

Scrapie is a transmissible neurodegenerative disease of sheep and goats. An abnormal host protein, Sp33-37, is the major protein component of the scrapie agent and the only known disease- or agent-specific macromolecule. Two monoclonal antibodies (MAbs), 4H8 (immunoglobulin G2b [IgG2b]) and 6B11 (IgG1), produced by immunizing mice with the intact hamster 263K scrapie agent protein, Sp33-37Ha, were found to have species specificity similar to that reported previously for MAb 3F4 (IgG2a), which was produced by using PrP-27-30 as the immunogen (R. J. Kascsak, R. Rubenstein, P. A. Merz, M. Tonna-DeMasi, R. Fersko, R. I. Carp, H. M. Wisniewski, and H. Diringer, J. Virol. 61:3688-3693, 1987). These antibodies all bound to Sp33-37 derived from hamster but not from mouse cells. Competitive binding assays demonstrated that all three MAbs bound to the same or overlapping sites on Sp33-37Ha. The molecular location of the epitope for these antibodies was determined to within 10 residues by using an antigen competition enzyme-linked immunosorbent assay in which synthetic peptides spanning Sp33-37Ha residues 79 to 93 or 84 to 93 specifically inhibited binding of these antibodies to plates coated with purified Sp33-37Ha. A synthetic peptide with the mouse-specific sequence (83 to 92) that differed from the hamster sequence by substitution at two positions (MetHa-87----LeuMo-86 and MetHa-90----ValMo-89) did not inhibit antibody binding to Sp33-37Ha. MAb 3F4 binding to hamster Sp33-37 was eliminated by chemical modification of Sp33-37Ha with diethylpyrocarbonate or succinic anhydride and by cleavage with CNBr or trypsin. The effect of diethylpyrocarbonate on MAb 3F4 binding was not reversed by hydroxylamine treatment. MAb 3F4 binding was not affected by prolonged exposure of Sp33-37Ha to 70% formic acid or by boiling in sodium dodecyl sulfate. We conclude that the epitope for these MAbs is a linear determinant that includes Met-87, Lys-88, and Met-90 and that Met-90 is probably the major species-specific determinant.

Amino Acid Sequence↗