Selective destruction of protein function by chromophore-assisted laser inactivation.
- 1 August 1988
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 85 (15) , 5454-5458
- https://doi.org/10.1073/pnas.85.15.5454
Abstract
Chromophore-assisted laser inactivation of protein function has been achieved. After a protein binds a specific ligand or antibody conjugated with malachite green (C.I. 42,000), it is selectively inactivated by laser irradiation at a wavelength of light absorbed by the dye but not significantly absorbed by cellular components. Ligand-bound proteins in solution and on the surfaces of cells can be denatured without other proteins in the same samples being affected. Chromophore-assisted laser inactivation can be used to study cell surface phenomena by inactivating the functions of single proteins on living cells, a molecular extension of cellular laser ablation. It has an advantage over genetics and the use of specific inhibitors in that the protein function of a single cell within the organism can be inactivated by focusing the laser beam.This publication has 6 references indexed in Scilit:
- A METHOD FOR THE RAPID DETERMINATION OF ALKALINE PHOSPHATASE WITH FIVE CUBIC MILLIMETERS OF SERUMPublished by Elsevier ,2021
- Characterization of the chicken erythrocyte anion exchange protein.Journal of Biological Chemistry, 1983
- Selective Photothermolysis: Precise Microsurgery by Selective Absorption of Pulsed RadiationScience, 1983
- Acetylcholinesterase of human erythrocytes and neuromuscular junctions: homologies revealed by monoclonal antibodies.Proceedings of the National Academy of Sciences, 1982
- Rapid Killing of Single Neurons by Irradiation of Intracellularly Injected DyeScience, 1979
- A rapid, simple radiometric assay for cholinesterase, suitable for multiple determinationsAnalytical Biochemistry, 1975