Effects of the extent of DNP substitution on the apparent affinity constant and cooperation between sites in the reactions od dinitrophenylated human serum albumin with anti-DNP and anti-HSA antibodies coupled to agarose

Esteban Celis, Rosalía Ridaura, Carlos Larralde

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7 Citations (Scopus)

Abstract

Increments in the extent of dinitrophenyl (DNP)* substitution of human serum albumin (HSA) increases the apparent affinity constant of its reaction with anti-DNP antibodies coupled to agarose and decreases that of its reaction with anti-HSA antibodies also fixed to the same solid phase. An ascending limb of the Scatchard plot in the low levels of bound ligand is described and is shown to be also dependent of the degree of DNP substitution of the antigen. Resulta are discussed as indicative of a probabilistic effect of the antigens' valence on the apparent affinity constant for antibodies coupled to agarose while the ascending limb of the Scatchard plots as compatible with cooperation between antibody active sites.

Original languageEnglish (US)
Pages (from-to)553-559
Number of pages7
JournalImmunochemistry
Volume14
Issue number7
DOIs
StatePublished - Jan 1 1977
Externally publishedYes

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Serum Albumin
Sepharose
Extremities
Antigens
Antibody Affinity
Antibodies
Anti-Idiotypic Antibodies
Catalytic Domain
Ligands

ASJC Scopus subject areas

  • Medicine(all)

Cite this

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title = "Effects of the extent of DNP substitution on the apparent affinity constant and cooperation between sites in the reactions od dinitrophenylated human serum albumin with anti-DNP and anti-HSA antibodies coupled to agarose",
abstract = "Increments in the extent of dinitrophenyl (DNP)* substitution of human serum albumin (HSA) increases the apparent affinity constant of its reaction with anti-DNP antibodies coupled to agarose and decreases that of its reaction with anti-HSA antibodies also fixed to the same solid phase. An ascending limb of the Scatchard plot in the low levels of bound ligand is described and is shown to be also dependent of the degree of DNP substitution of the antigen. Resulta are discussed as indicative of a probabilistic effect of the antigens' valence on the apparent affinity constant for antibodies coupled to agarose while the ascending limb of the Scatchard plots as compatible with cooperation between antibody active sites.",
author = "Esteban Celis and Rosal{\'i}a Ridaura and Carlos Larralde",
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T1 - Effects of the extent of DNP substitution on the apparent affinity constant and cooperation between sites in the reactions od dinitrophenylated human serum albumin with anti-DNP and anti-HSA antibodies coupled to agarose

AU - Celis, Esteban

AU - Ridaura, Rosalía

AU - Larralde, Carlos

PY - 1977/1/1

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N2 - Increments in the extent of dinitrophenyl (DNP)* substitution of human serum albumin (HSA) increases the apparent affinity constant of its reaction with anti-DNP antibodies coupled to agarose and decreases that of its reaction with anti-HSA antibodies also fixed to the same solid phase. An ascending limb of the Scatchard plot in the low levels of bound ligand is described and is shown to be also dependent of the degree of DNP substitution of the antigen. Resulta are discussed as indicative of a probabilistic effect of the antigens' valence on the apparent affinity constant for antibodies coupled to agarose while the ascending limb of the Scatchard plots as compatible with cooperation between antibody active sites.

AB - Increments in the extent of dinitrophenyl (DNP)* substitution of human serum albumin (HSA) increases the apparent affinity constant of its reaction with anti-DNP antibodies coupled to agarose and decreases that of its reaction with anti-HSA antibodies also fixed to the same solid phase. An ascending limb of the Scatchard plot in the low levels of bound ligand is described and is shown to be also dependent of the degree of DNP substitution of the antigen. Resulta are discussed as indicative of a probabilistic effect of the antigens' valence on the apparent affinity constant for antibodies coupled to agarose while the ascending limb of the Scatchard plots as compatible with cooperation between antibody active sites.

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