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61.
The iron-chelating agent desferrioxamine now finds extensive use in the treatment and diagnosis of aluminum-related diseases in renal patients. We review the chemistry and pharmacokinetics of desferrioxamine in chelation therapy for patients on hemodialysis. 相似文献
62.
KA Keay LJ Crowfoot NS Floyd LA Henderson MJ Christie R Bandler 《Canadian Metallurgical Quarterly》1997,762(1-2):61-71
Differentiating the binding properties of applied lectins should facilitate the selection of lectins for characterization of glycoreceptors on the cell surface. Based on the binding specificities studied by inhibition assays of lectin-glycan interactions, over twenty Gal and/or GalNAc specific lectins have been divided into eight groups according to their specificity for structural units (lectin determinants), which are the disaccharide as all or part of the determinants and of GalNAc alpha 1-->Ser (Thr) of the peptide chain. A scheme of codes for lectin determinants is illustrated as follows: (1) F (GalNAc alpha 1-->3GalNAc), Forssman specific disaccharide--Dolichos biflorus (DBL), Helix pomatia (HPL) and Wistaria floribunda (WFL) lectins. (2) A (GalNAc alpha 1-->3 Gal), blood group A specific disaccharide--Codium fragile subspecies tomentosoides (CFT), Soy bean (SBL), Vicia villosa-A4 (VVL-A4), and Wistaria floribunda (WFL) lectins. (3) Tn (GalNAc alpha 1-->Ser (Thr) of the protein core)--Vicia villosa B4 (VVL-B4), Salvia sclarea (SSL), Maclura pomifera (MPL), Bauhinia purpurea alba (BPL) and Artocarpus integrifolia (Jacalin, AIL). (4) T (Gal beta 1-->3GalNAc), the mucin type sugar sequences on the human erythrocyte membrane(T alpha), T antigen or the disaccharides at the terminal nonreducing end of gangliosides (T beta)--Peanut (PNA), Bauhinia purpurea alba (BPL), Maclura pomifera (MPL), Sophora japonica (SJL), Artocarpus lakoocha (Artocarpin) lectins and Abrus precatorius agglutinin (APA).(5) I and II (Gal beta 1-->3(4)GlcNAc)--the disaccharide residue at the nonreducing end of the carbohydrate chains derived from either N- or O-glycosidic linkage--Ricinus communis agglutinin (RCA1), Datura stramonium (TAL, Thorn apple), Erythrina cristagalli (ECL, Coral tree), and Geodia cydonium (GCL). (6) B (Gal alpha 1-->3Gal), human blood group B specific disaccharide--Griffonia(Banderiaea) simplicifolia B4 (GSI-B4). (7) E (Gal alpha 1-->4Gal), receptors for pathogenic E. coli agglutinin, Shiga toxin and Mistletoe toxic lectin-I (ML-I) and abrin-a. 相似文献
63.
A Lange M Walayat CM Turnbull P Palka P Mankad GR Sutherland MJ Godman 《Canadian Metallurgical Quarterly》1997,78(4):382-389
The properties of chemically cured and light-cured composite resins were recorded at baseline and at intervals over seven years, while the materials were exposed to controlled storage conditions as well as to various conditions typical of clinical situations. For chemically cured resins in clinical conditions, mechanical properties decreased, and working and setting times increased over four years; if refrigerated (controlled), properties remained constant past seven years. For light-cured resins, test results were constant over the entire seven-year test period regardless of storage conditions. An accelerated aging protocol was developed to allow for the evaluation of the relative storage stability of new and similar materials. 相似文献
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Crystal structure of TNF-alpha mutant R31D with greater affinity for receptor R1 compared with R2 总被引:2,自引:0,他引:2
Reed C; Fu ZQ; Wu J; Xue YN; Harrison RW; Chen MJ; Weber IT 《Protein engineering, design & selection : PEDS》1997,10(10):1101-1107
Crystal structures have been determined of recombinant human tumor necrosis
factor-alpha (TNF-alpha) and its R31D mutant that preferentially binds to
TNF receptor R1 with more than seven times the relative affinity of binding
to receptor R2. Crystals of the wild-type TNF were of space group
P4(1)2(1)2 and had unit cell dimensions of a = b = 94.7 and c = 117.4 A.
Refinement of the structure gave an R-factor of 22.3% at 2.5 A resolution.
The crystals of TNF R31D mutant diffracted to 2.3 A resolution, and were of
identical space group to the wild type with unit cell dimensions of a = b =
95.4 and c = 116.2 A, and the structure was refined to an R-factor of
21.8%. The trimer structures of the wild-type and mutant TNF were similar
with a root mean square (r.m.s.) deviation of 0.56 A for Calpha atoms;
however, the subunits within each trimer were more variable with an average
r.m.s. deviation of 1.00 A on Calpha atoms for pairwise comparison of
subunits. Model complexes of TNF with receptors R1 and R2 have been used to
predict TNF-receptor interactions. Arg31 in all three subunits of wild-type
TNF is predicted to form an ionic interaction with the equivalent glutamic
acid in both receptors R1 and R2. Asp31 of the TNF R31D mutant is predicted
to interact differently with the two receptors. The side chain of Asp31 in
two subunits of the TNF mutant is predicted to form hydrogen bond
interactions with Ser59 or Cys70 of R1, while it has no predicted
interactions with R2. The loss of three strong ionic interactions of Arg31
and the electrostatic repulsion of Asp31 with Glu in the receptors is
consistent with the reduced binding of the R31D mutant to both receptors
relative to wild-type TNF. The replacement of these ionic interactions by
two weaker hydrogen bond interactions between Asp31 of the R31D mutant and
R1, compared with no interactions with R2, is in agreement with the
observed preferential binding of the R31D mutant to R1 over R2. Analysis of
the structure and function of receptor-discriminating mutants of TNF will
help understand the biological role of TNF and facilitate its use as an
antitumor agent.
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