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Binding of pyrene isothiocyanate to the E1ATP site makes the H4‐H5 cytoplasmic loop of Na+/K+‐ATPase rigid
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| Zeitschriftentitel: | European Journal of Biochemistry |
|---|---|
| Personen und Körperschaften: | , , , , , , |
| In: | European Journal of Biochemistry, 251, 1998, 1-2, S. 522-527 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
|
| Schlagwörter: |
| author_facet |
Linnertz, Holger Miksik, Ivan Kvasnicka, Peter Bertoli, Enrico Mazzanti, Laura Schoner, Wilhelm Amler, Evzen Linnertz, Holger Miksik, Ivan Kvasnicka, Peter Bertoli, Enrico Mazzanti, Laura Schoner, Wilhelm Amler, Evzen |
|---|---|
| author |
Linnertz, Holger Miksik, Ivan Kvasnicka, Peter Bertoli, Enrico Mazzanti, Laura Schoner, Wilhelm Amler, Evzen |
| spellingShingle |
Linnertz, Holger Miksik, Ivan Kvasnicka, Peter Bertoli, Enrico Mazzanti, Laura Schoner, Wilhelm Amler, Evzen European Journal of Biochemistry Binding of pyrene isothiocyanate to the E1ATP site makes the H4‐H5 cytoplasmic loop of Na+/K+‐ATPase rigid Biochemistry |
| author_sort |
linnertz, holger |
| spelling |
Linnertz, Holger Miksik, Ivan Kvasnicka, Peter Bertoli, Enrico Mazzanti, Laura Schoner, Wilhelm Amler, Evzen 0014-2956 1432-1033 Wiley Biochemistry http://dx.doi.org/10.1046/j.1432-1327.1998.2510522.x <jats:p>1‐Pyreneisothiocyanate was shown to be an inhibitor of Na<jats:sup>+</jats:sup>/K<jats:sup>+</jats:sup>‐ATPase. Reverse‐phase HPLC and activity studies indicated binding of 1‐pyreneisothiocyanate at the H<jats:sub>4</jats:sub>‐H<jats:sub>5</jats:sub> loop of the α subunit and competition with the fluorescein 5′‐isothiocyanate for the E<jats:sub>1</jats:sub>ATP site. While fluorescein 5′‐isothiocyanate, the fluorescent ATP pseudo‐analog, was shown to be immobilized at the E<jats:sub>1</jats:sub>ATP site, there was no possibility to draw any conclusion about the flexibility of the E<jats:sub>1</jats:sub>ATP site due to its short lifetime. Employing 1pyreneisothiocyanate as a long‐lived fluorophore and a label for the E<jats:sub>1</jats:sub>ATP site, we found that the ATP‐binding site of Na<jats:sup>+</jats:sup>/K<jats:sup>+</jats:sup>‐ATPase and, in fact, the whole large intracellularly exposed H<jats:sub>4</jats:sub>‐H<jats:sub>5</jats:sub> loop of the catalytic α subunit is rigid and rotationally immobilized. This has important consequences for the molecular mechanism of the transport function.</jats:p> Binding of pyrene isothiocyanate to the E<sub>1</sub>ATP site makes the H<sub>4</sub>‐H<sub>5</sub> cytoplasmic loop of Na<sup>+</sup>/K<sup>+</sup>‐ATPase rigid European Journal of Biochemistry |
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10.1046/j.1432-1327.1998.2510522.x |
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Online Free |
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Chemie und Pharmazie |
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Wiley, 1998 |
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Wiley, 1998 |
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linnertz1998bindingofpyreneisothiocyanatetothee1atpsitemakestheh4h5cytoplasmicloopofnakatpaserigid |
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1998 |
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European Journal of Biochemistry |
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49 |
| title |
Binding of pyrene isothiocyanate to the E1ATP site makes the H4‐H5 cytoplasmic loop of Na+/K+‐ATPase rigid |
| title_unstemmed |
Binding of pyrene isothiocyanate to the E1ATP site makes the H4‐H5 cytoplasmic loop of Na+/K+‐ATPase rigid |
| title_full |
Binding of pyrene isothiocyanate to the E1ATP site makes the H4‐H5 cytoplasmic loop of Na+/K+‐ATPase rigid |
| title_fullStr |
Binding of pyrene isothiocyanate to the E1ATP site makes the H4‐H5 cytoplasmic loop of Na+/K+‐ATPase rigid |
| title_full_unstemmed |
Binding of pyrene isothiocyanate to the E1ATP site makes the H4‐H5 cytoplasmic loop of Na+/K+‐ATPase rigid |
| title_short |
Binding of pyrene isothiocyanate to the E1ATP site makes the H4‐H5 cytoplasmic loop of Na+/K+‐ATPase rigid |
| title_sort |
binding of pyrene isothiocyanate to the e<sub>1</sub>atp site makes the h<sub>4</sub>‐h<sub>5</sub> cytoplasmic loop of na<sup>+</sup>/k<sup>+</sup>‐atpase rigid |
| topic |
Biochemistry |
| url |
http://dx.doi.org/10.1046/j.1432-1327.1998.2510522.x |
| publishDate |
1998 |
| physical |
522-527 |
| description |
<jats:p>1‐Pyreneisothiocyanate was shown to be an inhibitor of Na<jats:sup>+</jats:sup>/K<jats:sup>+</jats:sup>‐ATPase. Reverse‐phase HPLC and activity studies indicated binding of 1‐pyreneisothiocyanate at the H<jats:sub>4</jats:sub>‐H<jats:sub>5</jats:sub> loop of the α subunit and competition with the fluorescein 5′‐isothiocyanate for the E<jats:sub>1</jats:sub>ATP site. While fluorescein 5′‐isothiocyanate, the fluorescent ATP pseudo‐analog, was shown to be immobilized at the E<jats:sub>1</jats:sub>ATP site, there was no possibility to draw any conclusion about the flexibility of the E<jats:sub>1</jats:sub>ATP site due to its short lifetime. Employing 1pyreneisothiocyanate as a long‐lived fluorophore and a label for the E<jats:sub>1</jats:sub>ATP site, we found that the ATP‐binding site of Na<jats:sup>+</jats:sup>/K<jats:sup>+</jats:sup>‐ATPase and, in fact, the whole large intracellularly exposed H<jats:sub>4</jats:sub>‐H<jats:sub>5</jats:sub> loop of the catalytic α subunit is rigid and rotationally immobilized. This has important consequences for the molecular mechanism of the transport function.</jats:p> |
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| author | Linnertz, Holger, Miksik, Ivan, Kvasnicka, Peter, Bertoli, Enrico, Mazzanti, Laura, Schoner, Wilhelm, Amler, Evzen |
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| description | <jats:p>1‐Pyreneisothiocyanate was shown to be an inhibitor of Na<jats:sup>+</jats:sup>/K<jats:sup>+</jats:sup>‐ATPase. Reverse‐phase HPLC and activity studies indicated binding of 1‐pyreneisothiocyanate at the H<jats:sub>4</jats:sub>‐H<jats:sub>5</jats:sub> loop of the α subunit and competition with the fluorescein 5′‐isothiocyanate for the E<jats:sub>1</jats:sub>ATP site. While fluorescein 5′‐isothiocyanate, the fluorescent ATP pseudo‐analog, was shown to be immobilized at the E<jats:sub>1</jats:sub>ATP site, there was no possibility to draw any conclusion about the flexibility of the E<jats:sub>1</jats:sub>ATP site due to its short lifetime. Employing 1pyreneisothiocyanate as a long‐lived fluorophore and a label for the E<jats:sub>1</jats:sub>ATP site, we found that the ATP‐binding site of Na<jats:sup>+</jats:sup>/K<jats:sup>+</jats:sup>‐ATPase and, in fact, the whole large intracellularly exposed H<jats:sub>4</jats:sub>‐H<jats:sub>5</jats:sub> loop of the catalytic α subunit is rigid and rotationally immobilized. This has important consequences for the molecular mechanism of the transport function.</jats:p> |
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| imprint_str_mv | Wiley, 1998 |
| institution | DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229 |
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| spelling | Linnertz, Holger Miksik, Ivan Kvasnicka, Peter Bertoli, Enrico Mazzanti, Laura Schoner, Wilhelm Amler, Evzen 0014-2956 1432-1033 Wiley Biochemistry http://dx.doi.org/10.1046/j.1432-1327.1998.2510522.x <jats:p>1‐Pyreneisothiocyanate was shown to be an inhibitor of Na<jats:sup>+</jats:sup>/K<jats:sup>+</jats:sup>‐ATPase. Reverse‐phase HPLC and activity studies indicated binding of 1‐pyreneisothiocyanate at the H<jats:sub>4</jats:sub>‐H<jats:sub>5</jats:sub> loop of the α subunit and competition with the fluorescein 5′‐isothiocyanate for the E<jats:sub>1</jats:sub>ATP site. While fluorescein 5′‐isothiocyanate, the fluorescent ATP pseudo‐analog, was shown to be immobilized at the E<jats:sub>1</jats:sub>ATP site, there was no possibility to draw any conclusion about the flexibility of the E<jats:sub>1</jats:sub>ATP site due to its short lifetime. Employing 1pyreneisothiocyanate as a long‐lived fluorophore and a label for the E<jats:sub>1</jats:sub>ATP site, we found that the ATP‐binding site of Na<jats:sup>+</jats:sup>/K<jats:sup>+</jats:sup>‐ATPase and, in fact, the whole large intracellularly exposed H<jats:sub>4</jats:sub>‐H<jats:sub>5</jats:sub> loop of the catalytic α subunit is rigid and rotationally immobilized. This has important consequences for the molecular mechanism of the transport function.</jats:p> Binding of pyrene isothiocyanate to the E<sub>1</sub>ATP site makes the H<sub>4</sub>‐H<sub>5</sub> cytoplasmic loop of Na<sup>+</sup>/K<sup>+</sup>‐ATPase rigid European Journal of Biochemistry |
| spellingShingle | Linnertz, Holger, Miksik, Ivan, Kvasnicka, Peter, Bertoli, Enrico, Mazzanti, Laura, Schoner, Wilhelm, Amler, Evzen, European Journal of Biochemistry, Binding of pyrene isothiocyanate to the E1ATP site makes the H4‐H5 cytoplasmic loop of Na+/K+‐ATPase rigid, Biochemistry |
| title | Binding of pyrene isothiocyanate to the E1ATP site makes the H4‐H5 cytoplasmic loop of Na+/K+‐ATPase rigid |
| title_full | Binding of pyrene isothiocyanate to the E1ATP site makes the H4‐H5 cytoplasmic loop of Na+/K+‐ATPase rigid |
| title_fullStr | Binding of pyrene isothiocyanate to the E1ATP site makes the H4‐H5 cytoplasmic loop of Na+/K+‐ATPase rigid |
| title_full_unstemmed | Binding of pyrene isothiocyanate to the E1ATP site makes the H4‐H5 cytoplasmic loop of Na+/K+‐ATPase rigid |
| title_short | Binding of pyrene isothiocyanate to the E1ATP site makes the H4‐H5 cytoplasmic loop of Na+/K+‐ATPase rigid |
| title_sort | binding of pyrene isothiocyanate to the e<sub>1</sub>atp site makes the h<sub>4</sub>‐h<sub>5</sub> cytoplasmic loop of na<sup>+</sup>/k<sup>+</sup>‐atpase rigid |
| title_unstemmed | Binding of pyrene isothiocyanate to the E1ATP site makes the H4‐H5 cytoplasmic loop of Na+/K+‐ATPase rigid |
| topic | Biochemistry |
| url | http://dx.doi.org/10.1046/j.1432-1327.1998.2510522.x |