PubMed Health⌕ Search

Biomedical subjects

B A Baird

Publications and source records attributed to B A Baird.

8 recordsLinked to original sources
PubMed1999

Interleukin 1 (IL-1) causes changes in lateral and rotational mobilities of IL-1 type I receptors.

To investigate IL-1-dependent interactions of IL-1 type I (IL-1 RI) receptors on intact cells, lateral and rotational mobilities and detergent insolubility were investigated. Lateral mobility was measured by fluorescence photobleaching recovery, using a Cy3-modified, noncompetitive mAb specific for IL-1RI (M5) bound to wild-type IL-1 RI or mutant IL-1 RI with a truncated cytoplasmic tail. Addition of IL-1 causes significant reduction in the mobile fraction of wild-type IL-1 RI for two different transfected cell lines. For the mutant IL-1 RI, no significant decrease in response to IL-1 is observed, indicating that the missing cytoplasmic segment is involved in IL-1-dependent interactions of IL-1 RI that lead to reduced lateral mobility on the cell surface. The rotational mobility of IL-1 RI was assessed with phosphorescence anisotropy decay measurements using erythrosin-labeled M5. IL-1 decreases the rotational mobility of cell surface IL-1 RI on the microsecond time scale and also increases the initial anisotropy, indicating loss in segmental motion. Measurements of resistance to solubilization by Triton X-100 showed that IL-1 binding increases the fraction of IL-1 RI sedimenting with cytoskeletal residues. The IL-1 receptor antagonist protein (IL-1ra) causes partial effects in reducing rotational mobility and increasing detergent insolubility of M5-lableled IL-1 RI, indicating that this ligand causes structural changes in the presence of the dimerizing M5 mAb. These ligand-dependent physical interactions of IL-1 RI on the cell surface may be related to signal initiation by this receptor.

Animals↗
PubMed1979

The optimal amino acid supplementation of barley for the growing pig. 1. Response of nitrogen metabolism to progressive supplementation.

1. In five experiments, involving 142 female pigs weighing on average 33 kg, estimates were made of the amounts of essential amino acids which minimized urinary N excretion when diets with barley as the only source of protein were given at the rate of 120 g/kg0.75 per d. 2. With additions of lysine (4.0 g/kg diet) and threonine, (1.2 g/kg diet) to barley urinary N excretion decreased from 0.91 to 0.36 g/kg0.75 per d, corresponding to an increase in biological value (bv) from 0.51 to 0.86. 3. With these additions of lysine and threonine, there were no responses to additions of tryptophan, methionine or isoleucine, or to further additions of lysine or threonine, but addition of histidine significantly reduced N excretion. 4. No optimal addition of histidine could be determined; the mean rate of N excretion after addition of histidine (not less than 0.3 g/kg diet) was 0.27 g/kg0.75 per d, corresponding to a BV of 0.93. 5. There was a variation between pigs from different litters in their responses to added histidine. Those with low rates of N excretion on the unsupplemented diet did not respond to additions of histidine, but those with high rates did. 6. It is concluded that additions of only three amino acids can greatly improve the nutritive value of barley protein for the growing pig and that the amino acid composition of the supplemented protein closely approaches the ideal; it is also similar to whole-body tissue protein.

Amino Acids, Essential↗
PubMed1976

Chemical cross-linking studies of chloroplast coupling factor 1.

Cross-linking reagents have been used to link covalently adjacent subunits of solubilized spinach chloroplast coupling factor 1, which is a latent ATPase. 1,5-Difluoro-2,4-dinitrobenzene, dimethyl-3,3'-dithiobispropionimidate, and dimethylsuberimidate are able to form bridges of 3 to 11 A between amino groups, and hydrogen peroxide and the o-phenanthroline-cupric ion complex catalyze the oxidation of intrinsic sulfhydryl groups. The five individual subunit bands (alpha, beta, gamma, delta, and epsilon) and several new aggregate bands can be separated by means of sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The same four fastest moving aggregate bands, as characterized by their mobilities, migrate more slowly than the heaviest subunit band and appear with all of the cross-linkers employed. The subunit composition of the aggregate bands has been determined through the use of the reversible cross-linkers, dimethyldithiobispropionimidate, (o-phenanthroline)2Cu(II), and H2O2, and two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis in which aggregates are separated in the first dimension, the disulfide cross-links are cleaved, and the individual subunits present in the aggregates are separated in the second dimension. The subunits are detected by Coomassie brilliant blue staining and by labeling some of the sulfhydryl groups of the gamma and epsilon subunits with radioactive N-ethylmaleimide. The results obtained indicate that the alpha and beta subunits can cross-link directly with each of the other subunits, that two beta subunits are adjacent, and that gamma epsilon, gamma epsilon 2, alpha delta, and beta delta aggregates are present. A minimal subunit stoichiometry consistent with these results is alpha 2 beta 2 gamma delta epsilon 2. A possible structural model of the coupling factor is derived from the data. Similar, but less extensive, experiments have been carried out with the heat-activated coupling factor (which is an ATPase); no differences in the spatial arrangement of subunits are detected from the two-dimensional gel electrophoresis analysis of the cross-linked aggregates.

Adenosine Triphosphatases↗