Výsledky vyhledávání - "D. T. B. Shih"

Altered Ligand Rebinding Kinetics Due to Distal-side Effects in Hemoglobin Chico (Lysβ66(E10) → Thr)

Autor: Joel M. Friedman, D. T.-B. Shih, E. T. Iben, Celia Bonaventura, Joseph Bonaventura

Publikováno v: Journal of Biological Chemistry. 274:8686-8693

Hb Chico is an unusual human hemoglobin variant that has lowered oxygen affinity, but unaltered cooperativity and anion sensitivity. Previous studies showed these features to be associated with distal-side heme pocket alterations that confer increase

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e7e0eeeb0cc0fcefde06ffa2db7b0bd
https://doi.org/10.1074/jbc.274.13.8686

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Involvement of the distal histidine in the low affinity exhibited by Hb Chico (Lys beta 66—-Thr) and its isolated beta chains

Autor: D. T.-B. Shih, G. Fermi, Celia Bonaventura, Joseph Bonaventura, M. Perutz, Robert Cashon

Publikováno v: Journal of Biological Chemistry. 266:23033-23040

Hemoglobin (Hb) Chico (Lys beta 66----Thr at E10) has a diminished oxygen affinity (Shih, D. T.-b., Jones, R. T., Shih, M. F.-C., Jones, M. B., Koler, R. D., and Howard, J. (1987) Hemoglobin 11, 453-464). Our studies show that its P50 is about twice

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ef377d4c6069ab0374ebdc19d36b895e
https://doi.org/10.1016/s0021-9258(18)54459-8

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ISOLATION AND CHARACTERIZATION OF STEM/ PROGENITOR CELLS FROM HUMAN AMNION – POSSIBLE APPLICATION OF NEURAL REPAIR IN THE FUTURE

Autor: D. T. B. Shih, C. C. Hsiao, E. Y. Shen, D. C. Lee, W. T. Chiu, C. T. Huang, S. M. Weng, C. S. Hsu

Publikováno v: Neuropediatrics. 37

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::67ba4930bfe0a0a25679e88f24f5410e
https://doi.org/10.1055/s-2006-943698

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The pKa values of two histidine residues in human haemoglobin, the Bohr effect, and the dipole moments of α-helices

Autor: J.H. Fogg, D. T.-B. Shih, G.M. Clore, Angela M. Gronenborn, Max F. Perutz

Publikováno v: Journal of Molecular Biology. 183:491-498

Studies of abnormal and chemically modified haemoglobins indicate that in 0.1 M-NaCl about 40% of the alkaline Bohr effect of human haemoglobin is contributed by the C-terminal histidine HC3(146) beta. In deoxyhaemoglobin, the imidazole of this histi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa46c543a862a2fdd1fcfdeef5213f27
https://doi.org/10.1016/0022-2836(85)90016-6

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Influence of anions and protons on the adair coefficients of haemoglobins A and Cowtown (His HC3(146)β → leu)

Autor: D. T.-B. Shih, Max F. Perutz

Publikováno v: Journal of Molecular Biology. 195:419-422

We have measured the contribution of the alkaline Bohr effect of the C-terminal histidine residues of the beta-chains of haemoglobin A by comparing haemoglobin A with haemoglobin Cowtown in which those histidine residues are replaced by leucine. Oxyg

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https://doi.org/10.1016/0022-2836(87)90660-7

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Histidine proton resonances of carbonmonoxyhaemoglobins A and Cowtown in chloride-free buffer

Autor: D. T.-B. Shih, M F Peratz, Clore Gm, Angela M. Gronenborn

Publikováno v: Journal of Molecular Biology. 195:453-455

A re-examination of the C-2 histidine proton resonances of haemoglobins A and Cowtown (His HC3(146) beta----Leu) in chloride-free Hepes buffer has shown that all the resonances present in haemoglobin A are present in haemoglobin Cowtown, so that the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8d5a06caf7e2a7db36f089f720ee84c7
https://doi.org/10.1016/0022-2836(87)90666-8

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Modification of hemoglobin with site-directed bifunctional reagents

Autor: D. T.-B. Shih, M.P. Kavanaugh, R.T. Jones

Publikováno v: Acta haematologica. 78(2-3)

Reaction of deoxy-Hb with the periodate-oxidized derivatives of nicotinamide adenine dinucleotide (o-NAD), phosphoribosyl pyrophosphate (o-PRPP), adenosine triphosphate (o-ATP), glucose-1-phosphate (o-glc-1-P) and nicotinamide adenine dinucleotide ph

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::43fa30c4aeef536c3f7554ec166918cd
https://pubmed.ncbi.nlm.nih.gov/3120483

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Chemical Modification of Hemoglobin with 4,4′-Diisothiocyanostilbene-2,2′-Disulfonate (DIDS): Initial Studies of a Potential Blood Substitute

Autor: R. T. Jones, B. Hedlund, D. T.-B. Shih, M. P. Kavanaugh

Publikováno v: Biomaterials, Artificial Cells and Artificial Organs. 16:637-637

Several bifunctional 2,3-diphosphoglycerate (DPG) analogs will cross-link residues in the DPG binding site and prevent subunit dissociation of undenatured hemoglobin. By selecting reagents of proper structure and appropriate reaction conditions, it i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::52f198b1a8a07dce1c1501cdd62c5c18
https://doi.org/10.3109/10731198809132623

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