Affinity Labeling of Receptors for Steroid and Thyroid Hormones

John A. Katzenellenbogen, Benita S Katzenellenbogen

Research output: Contribution to journalArticle

Abstract

This chapter discusses the affinity labeling of receptors for steroid and thyroid hormones. Affinity labeling is a technique for the selective, covalent labeling of binding sites in macromolecules. It involves initially the reversible binding of an affinity probe, which is a ligand modified to contain a reactive functional group (attaching function), within the binding site of the macromolecule, followed then by the covalent attachment of the affinity probe to the molecular constituents within or near the binding site. The selectivity of the labeling process derives from the selective interaction of the affinity probe with the binding site. The labeling of receptors for hormones generally requires that a very small quantity of protein, generally present as a very minor component in a heterogeneous binding preparation, undergo covalent interaction with the affinity probe. For this to be done successfully, or at best optimally, the labeling process must be both efficient—that is, as much as possible (ideally all) of the receptor should become labeled—and selective—that is, as little as possible of the other non-receptor proteins should become labeled.

Original languageEnglish (US)
Pages (from-to)213-281
Number of pages69
JournalVitamins and Hormones
Volume41
Issue numberC
DOIs
StatePublished - Jan 1 1984

Fingerprint

Thyroid Hormone Receptors
Binding Sites
Molecular Probes
Proteins
Hormones
Ligands

ASJC Scopus subject areas

  • Physiology
  • Endocrinology

Cite this

Affinity Labeling of Receptors for Steroid and Thyroid Hormones. / Katzenellenbogen, John A.; Katzenellenbogen, Benita S.

In: Vitamins and Hormones, Vol. 41, No. C, 01.01.1984, p. 213-281.

Research output: Contribution to journalArticle

@article{a1a40169a51d448791f4ae9206db9607,
title = "Affinity Labeling of Receptors for Steroid and Thyroid Hormones",
abstract = "This chapter discusses the affinity labeling of receptors for steroid and thyroid hormones. Affinity labeling is a technique for the selective, covalent labeling of binding sites in macromolecules. It involves initially the reversible binding of an affinity probe, which is a ligand modified to contain a reactive functional group (attaching function), within the binding site of the macromolecule, followed then by the covalent attachment of the affinity probe to the molecular constituents within or near the binding site. The selectivity of the labeling process derives from the selective interaction of the affinity probe with the binding site. The labeling of receptors for hormones generally requires that a very small quantity of protein, generally present as a very minor component in a heterogeneous binding preparation, undergo covalent interaction with the affinity probe. For this to be done successfully, or at best optimally, the labeling process must be both efficient—that is, as much as possible (ideally all) of the receptor should become labeled—and selective—that is, as little as possible of the other non-receptor proteins should become labeled.",
author = "Katzenellenbogen, {John A.} and Katzenellenbogen, {Benita S}",
year = "1984",
month = "1",
day = "1",
doi = "10.1016/S0083-6729(08)60091-6",
language = "English (US)",
volume = "41",
pages = "213--281",
journal = "Vitamins and Hormones",
issn = "0083-6729",
publisher = "Academic Press Inc.",
number = "C",

}

TY - JOUR

T1 - Affinity Labeling of Receptors for Steroid and Thyroid Hormones

AU - Katzenellenbogen, John A.

AU - Katzenellenbogen, Benita S

PY - 1984/1/1

Y1 - 1984/1/1

N2 - This chapter discusses the affinity labeling of receptors for steroid and thyroid hormones. Affinity labeling is a technique for the selective, covalent labeling of binding sites in macromolecules. It involves initially the reversible binding of an affinity probe, which is a ligand modified to contain a reactive functional group (attaching function), within the binding site of the macromolecule, followed then by the covalent attachment of the affinity probe to the molecular constituents within or near the binding site. The selectivity of the labeling process derives from the selective interaction of the affinity probe with the binding site. The labeling of receptors for hormones generally requires that a very small quantity of protein, generally present as a very minor component in a heterogeneous binding preparation, undergo covalent interaction with the affinity probe. For this to be done successfully, or at best optimally, the labeling process must be both efficient—that is, as much as possible (ideally all) of the receptor should become labeled—and selective—that is, as little as possible of the other non-receptor proteins should become labeled.

AB - This chapter discusses the affinity labeling of receptors for steroid and thyroid hormones. Affinity labeling is a technique for the selective, covalent labeling of binding sites in macromolecules. It involves initially the reversible binding of an affinity probe, which is a ligand modified to contain a reactive functional group (attaching function), within the binding site of the macromolecule, followed then by the covalent attachment of the affinity probe to the molecular constituents within or near the binding site. The selectivity of the labeling process derives from the selective interaction of the affinity probe with the binding site. The labeling of receptors for hormones generally requires that a very small quantity of protein, generally present as a very minor component in a heterogeneous binding preparation, undergo covalent interaction with the affinity probe. For this to be done successfully, or at best optimally, the labeling process must be both efficient—that is, as much as possible (ideally all) of the receptor should become labeled—and selective—that is, as little as possible of the other non-receptor proteins should become labeled.

UR - http://www.scopus.com/inward/record.url?scp=0021646976&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021646976&partnerID=8YFLogxK

U2 - 10.1016/S0083-6729(08)60091-6

DO - 10.1016/S0083-6729(08)60091-6

M3 - Article

C2 - 6099632

AN - SCOPUS:0021646976

VL - 41

SP - 213

EP - 281

JO - Vitamins and Hormones

JF - Vitamins and Hormones

SN - 0083-6729

IS - C

ER -