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Archivo Fotográfico

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View from left (south) of the convocation stage during the 1970 Spring Convocation.

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One of the various functions of proteins in biological systems is the transport of small molecules, for this purpose proteins have naturally evolved special mechanisms to allow both ligand binding and its subsequent release to a target site; a process fundamental to many biological processes. Transport of Vitamin E (a-tocopherol), a lipid soluble antioxidant, to membranes helps in the protection of polyunsaturated fatty acids against peroxidative damage. In this research, the ligand binding characteristics of several members of the CRALTRIO family of lipid binding proteins was examined; the recombinant human a-Tocopherol Transfer Protein (a-TIP), Supernatant Protein Factor (SPF)ffocopherol Associated Protein (TAP), Cellular Retinaldehyde Binding Protein (CRALBP) and the phosphatidylinositol transfer protein from S. cerevisiae Sec 14p. Recombinant Sec 14p was expressed and purified from E. coli for comparison of tocopherol binding to the two other recombinant proteins postulated to traffic a-tocopherol. Competitive binding assays using [3H]-a-tocopherol and Lipidex-l000 resin allowed determination of the dissociation constants ~) of the CRAL-TRIO proteins for a-tocopherol and - 20 hydrophobic ligands for evaluation of the possible biological relevance of the binding interactions observed. The KIs (nM) for RRR-a-tocopherol are: a-TIP: 25.0, Sec 14p: 373, CRALBP: 528 and SPFffAP: 615. This indicates that all proteins recognize tocopherol but not with the same affinity. Sec 14p bound its native ligand PI with a KI of381 whereas SPFffAP bound PI (216) and y-tocopherol (268) similarly in contrast to the preferential binding ofRRR-a-tocopherol by a-TIP. Efforts to adequately represent biologically active SPFff AP involved investigation of tocopherol binding for several different recombinant proteins derived from different constructs and in the presence of different potential modulators (Ca+2, Mg+2, GTP and GDP); none of these conditions enhanced or inhibited a-tocopherol binding to SPF. This work suggests that only aTTP serves as the physiological mediator of a-tocopherol, yet structural homology between proteins allows common recognition of similar ligand features. In addition, several photo-affmity analogs of a-tocopherol were evaluated for their potential utility in further elucidation of a-TTP function or identification of novel tocopherol binding proteins.

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Consists of 33 postcards featuring various scenes and landmarks in the Niagara region. The postcards feature the Great Gorge Route, the Niagara River and Falls, Queenston Heights, Ridley College, military camps in Niagara-on-the-Lake, and a Catholic Church in Port Colborne. Most of the postcards are blank, but four have been postmarked. One of these is addressed to Miss Ada Misner, Espanola, Ont., from M.G. and is postmarked August 18, 1908. Another postcard is addressed to Mr. Alfred H. Smith, Stamford Hill, London N., from Hedley Smith, France and is postmarked 1902. Another is addressed to Miss Annabel Bishop, Buffalo, N.Y. from Irene Lalour(?), and is postmarked April 30, 1908. The last postcard is addressed to Miss Edna Lackie, Toronto, from R.M. and is postmarked August 1, 1910.

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UANL

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UANL

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UANL