Výsledky vyhledávání - "D B McIntosh"

Catalysis of an ATP analogue untethered and tethered to lysine 492 of sarcoplasmic reticulum Ca(2+)-ATPase

Autor: D B, McIntosh, D G, Woolley

Publikováno v: The Journal of biological chemistry. 269(34)

2',3'-O-(2,4,6-trinitrophenyl)-8-azido-AMP (TNP-8N3-AMP) and -ATP photolabel Lys-492 at the active site of the Ca(2+)-ATPase of sarcoplasmic reticulum (McIntosh, D. B., Woolley, D. G., and Berman, M. C. (1992) J. Biol. Chem. 267, 5301-5309). We now f

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c701794419781f29d391402c87ab1bb4
https://pubmed.ncbi.nlm.nih.gov/8063798

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Glutaraldehyde cross-links Lys-492 and Arg-678 at the active site of sarcoplasmic reticulum Ca(2+)-ATPase

Autor: D B, McIntosh

Publikováno v: The Journal of biological chemistry. 267(31)

It has been shown previously that glutaraldehyde cross-links the Ca(2+)-ATPase of sarcoplasmic reticulum intramolecularly at the active site, involving residues participating in nucleotide binding and the conformational change that results in Ca2+ re

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5c8872fdeaf83e67a6584016c09df644
https://pubmed.ncbi.nlm.nih.gov/1429585

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2',3'-O-(2,4,6-trinitrophenyl)-8-azido-AMP and -ATP photolabel Lys-492 at the active site of sarcoplasmic reticulum Ca(2+)-ATPase

Autor: D B, McIntosh, D G, Woolley, M C, Berman

Publikováno v: The Journal of biological chemistry. 267(8)

2',3'-O-(2,4,6-trinitrophenyl)-8-azido (TNP-8N3)-AMP, -ADP, and -ATP bind tightly to the Ca(2+)-ATPase of skeletal muscle sarcoplasmic reticulum and become covalently attached on irradiation at alkaline pH, concomitant with inactivation of ATPase act

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::81a446233a104ce3cd73da3fc7475dc9
https://pubmed.ncbi.nlm.nih.gov/1476544

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Mechanism of inhibition of sarcoplasmic reticulum Ca2(+)-ATPase by active site cross-linking. Impairment of nucleotide binding slows nucleotide-dependent phosphoryl transfer, and loss of active site flexibility stabilizes occluded forms and blocks E2-P formation

Autor: D C, Ross, G A, Davidson, D B, McIntosh

Publikováno v: The Journal of biological chemistry. 266(7)

Investigation of the properties of Ca2(+)-ATPase of sarcoplasmic reticulum cross-linked at the active site with glutaraldehyde showed that ATP binding affinity and rate of ATP-dependent phosphorylation and Ca2+ occlusion were decreased 2-3 orders of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::cc9e46e441b675691a7860795a28385d
https://pubmed.ncbi.nlm.nih.gov/1825656

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