| Autor: |
Wassef NM; Department of Membrane Biochemistry, Walter Reed Army Institute of Research, Washington, DC 20307-5100., Swartz GM, Alving BM, Alving CR |
| Jazyk: |
angličtina |
| Zdroj: |
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1993 Jan 29; Vol. 190 (2), pp. 582-8. |
| DOI: |
10.1006/bbrc.1993.1088 |
| Abstrakt: |
We have previously reported that each of four monoclonal antibodies to a phospholipid, phosphatidylinositol phosphate (PIP), has a phosphate binding subsite in the antigen binding site that can bind ATP (Molec. Immunol. 21, 863-868, 1984). We have now observed that antibody-bound ATP has the ability to donate a phosphate group in the phosphorylation reaction of glucose to glucose-6-phosphate catalyzed by hexokinase. The phosphorylation reaction proceeds equally efficiently when ATP is provided as free (nonbound) ATP or as antibody-bound ATP. We conclude that an anti-phospholipid antibody can serve as a carrier of a functionally active nucleotide. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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