Two-stage photosensitive label for antibody combining sites

Converse, Carolyn A.; Richards, Frederic M.

doi:10.1021/bi00839a031

Cited by 46 publications

(17 citation statements)

References 36 publications

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“…Photoreactive compounds containing azido group are widely used for the affinity label!ing of proteins [1][2][3][4]. Recently ATP-7-p-azidoanilidate* was found to be competitive inhibitor of ATP for phenylalanyltRNA synthetase (EC 6.1.1.)…”

Section: Introductionmentioning

confidence: 99%

Investigation of the phenylalanyl‐tRNA synthetase modification with γ‐(p‐Azidoanilide)‐ATP

Ankilova¹,

Knorre²,

Kravchenko³

et al. 1975

FEBS Letters

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Section: Introductionmentioning

confidence: 99%

Investigation of the phenylalanyl‐tRNA synthetase modification with γ‐(p‐Azidoanilide)‐ATP

Ankilova¹,

Knorre²,

Kravchenko³

et al. 1975

FEBS Letters

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“…The use of the triplet of benzophenone has also been suggested as a photochemical probe of biological ligand-receptor interactions (12). Among numerous applications of photoaffinity labeling are the covalent attachment of NAD+ analogs to enzymes (5,15), the identification of antibody binding sites (8,10), the labeling of phosphofructokinase with a cAMP analog (9), and the use of photosensitive analogs for study of estrogen binding proteins of the rat uterus (19,20).…”

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confidence: 99%

Photoaffinity-labeled Auxins

et al. 1975

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Two light-sensitive analogs of 2, 4-dichlorophenoxyacetic acid, namely 4-azido-2-chlorophenoxyacetic acid and 3-azido-5-chlorophenoxyacetic acid, have been synthesized for use as auxin photoaffinity labels. The preparation and biological activity of the compounds are described. Both contain the photolabile azido group; the 2,4-substituted compound shows auxin activity and the 3,5-substituted compound does not. These photoaffinity analogs of 2, 4-dichlorophenoxyacetic acid may be useful in the identification of the auxin receptor molecules in plant cells and eventually of the receptor sites within these molecules.Among plant growth regulators, the auxins are generally distinguished by their promotion of cell elongation (25,29

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“…An important variant of this method is photoaffinity labeling (4,5) in which a labeling reagent R-P is used, where P now is a group that is chemically unreactive in the dark, but upon photolysis is converted to an extremely reactive intermediate P*. In principle, P* may react to form a covalent bond with some group in the active site before R-P* can dissociate from the site.…”

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confidence: 99%

“…In principle, P* may react to form a covalent bond with some group in the active site before R-P* can dissociate from the site. Since the introduction of photolyzable reagents into site-labeling studies by Westheimer and his colleagues (6), several investigations (4,5,(7)(8)(9) have used this approach. In initial studies from this laboratory (7), we showed that the acetylcholinesterase (AChE; EC 3.1.1.7) activity of intact human erythrocyte membranes and the acetylcholine receptor (AChR) activity of frog sartorius muscle could be specifically and irreversibly inactivated by photolysis in the presence of either of two aryl azides, 4-azido,2-nitrobenzyltrimethylammonium (HK-83) or 4-azido,2-nitrobenzyltriethylammonium (HK-68) (Fig.…”

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confidence: 99%

The Mechanism of Photoaffinity Labeling

Ruoho

Kiefer

Roeder

et al. 1973

Proc. Natl. Acad. Sci. U.S.A.

139

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Photoaffinity labeling is a recently introduced method for covalently binding chemical tags to the active sites of protein molecules, which is potentially capable of very great specificities of labeling. A labeling reagent is used that is converted by photolysis to an extremely reactive intermediate. According to the expected mechanism, the reagent molecules that are specifically and reversibly bound to the active site at the instant of photolysis react irreversibly in the site before they can dissociate from the site. In two such reagent-protein systems studied in this paper, however, it is shown that, while by the usual criteria photoaffinity labeling appears to have occurred, the expected mechanism in fact does not hold. This was discovered in experiments with scavengers present in the mixtures that were photolyzed. The general properties of, and criteria for, photoaffinity labeling reactions are discussed in the light of these findings.

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Two-stage photosensitive label for antibody combining sites

Cited by 46 publications

References 36 publications

Investigation of the phenylalanyl‐tRNA synthetase modification with γ‐(p‐Azidoanilide)‐ATP

Investigation of the phenylalanyl‐tRNA synthetase modification with γ‐(p‐Azidoanilide)‐ATP

Photoaffinity-labeled Auxins

The Mechanism of Photoaffinity Labeling

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