Measurement of binding constants for divalent antibody-immobilized antigen interaction by antigen-sepharose 4b chromatography

María Rut Bruera; Daniel Sevlever; Carlos A. Gatti

doi:10.3109/08820138309051970

Measurement of binding constants for divalent antibody-immobilized antigen interaction by antigen-sepharose 4b chromatography

María Rut Bruera, Daniel Sevlever, Carlos A. Gatti

Neuroscience

Research output: Contribution to journal › Article › peer-review

2 Scopus citations

Abstract

Binding constants for the human IgG-anti human IgG heavy chain were determined from elution profiles obtained by loading human IgG-Sepharose 4B columns with the antibody and eluting it at different NaI concentrations. The agreement between the value obtained at zero NaI concentration and the value determined in solution by equilibrium molecular sieving was good. An application of this column method should be useful for comparison of avidity values of antibody populations of the same specificity.

Original language	English (US)
Pages (from-to)	529-538
Number of pages	10
Journal	Immunological Investigations
Volume	12
Issue number	5
DOIs	https://doi.org/10.3109/08820138309051970
State	Published - 1983

ASJC Scopus subject areas

Immunology

Access to Document

10.3109/08820138309051970

Cite this

@article{18f4701560e7482dbc0b54bc95f56b75,

title = "Measurement of binding constants for divalent antibody-immobilized antigen interaction by antigen-sepharose 4b chromatography",

abstract = "Binding constants for the human IgG-anti human IgG heavy chain were determined from elution profiles obtained by loading human IgG-Sepharose 4B columns with the antibody and eluting it at different NaI concentrations. The agreement between the value obtained at zero NaI concentration and the value determined in solution by equilibrium molecular sieving was good. An application of this column method should be useful for comparison of avidity values of antibody populations of the same specificity.",

author = "Bruera, {Mar{\'i}a Rut} and Daniel Sevlever and Gatti, {Carlos A.}",

year = "1983",

doi = "10.3109/08820138309051970",

language = "English (US)",

volume = "12",

pages = "529--538",

journal = "Immunological Investigations",

issn = "0882-0139",

publisher = "Informa Healthcare",

number = "5",

}

TY - JOUR

T1 - Measurement of binding constants for divalent antibody-immobilized antigen interaction by antigen-sepharose 4b chromatography

AU - Bruera, María Rut

AU - Sevlever, Daniel

AU - Gatti, Carlos A.

PY - 1983

Y1 - 1983

N2 - Binding constants for the human IgG-anti human IgG heavy chain were determined from elution profiles obtained by loading human IgG-Sepharose 4B columns with the antibody and eluting it at different NaI concentrations. The agreement between the value obtained at zero NaI concentration and the value determined in solution by equilibrium molecular sieving was good. An application of this column method should be useful for comparison of avidity values of antibody populations of the same specificity.

AB - Binding constants for the human IgG-anti human IgG heavy chain were determined from elution profiles obtained by loading human IgG-Sepharose 4B columns with the antibody and eluting it at different NaI concentrations. The agreement between the value obtained at zero NaI concentration and the value determined in solution by equilibrium molecular sieving was good. An application of this column method should be useful for comparison of avidity values of antibody populations of the same specificity.

UR - http://www.scopus.com/inward/record.url?scp=84907110109&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84907110109&partnerID=8YFLogxK

U2 - 10.3109/08820138309051970

DO - 10.3109/08820138309051970

M3 - Article

AN - SCOPUS:84907110109

SN - 0882-0139

VL - 12

SP - 529

EP - 538

JO - Immunological Investigations

JF - Immunological Investigations

IS - 5

ER -

Measurement of binding constants for divalent antibody-immobilized antigen interaction by antigen-sepharose 4b chromatography

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this