Advanced

Quantitation of protein A in human plasma is possible after heat inactivation of the samples

Nilsson, Rune LU and Davidsson, Bertil (1990) In Journal of Immunological Methods 135(1-2). p.77-80
Abstract
Quantitative determination of staphylococcal protein A in plasma is often hampered by the interaction between protein A and immunoglobulins. In human plasma, these interactions may not only involve the non-immune binding to the Fc or Fab regions of Ig but also antigen/antibody interaction by specific antibodies directed against protein A. In this paper we describe a method which can be used to quantitate nanogram amounts of protein A in the presence of human plasma. The ELISA used for the quantification of protein A is based on a double antibody solid-phase assay utilizing chicken anti-protein A as both capture and detector antibody. Protein A may be measured down to 5 ng/ml in plasma and 0.5 ng/ml in buffer. The plasma samples were... (More)
Quantitative determination of staphylococcal protein A in plasma is often hampered by the interaction between protein A and immunoglobulins. In human plasma, these interactions may not only involve the non-immune binding to the Fc or Fab regions of Ig but also antigen/antibody interaction by specific antibodies directed against protein A. In this paper we describe a method which can be used to quantitate nanogram amounts of protein A in the presence of human plasma. The ELISA used for the quantification of protein A is based on a double antibody solid-phase assay utilizing chicken anti-protein A as both capture and detector antibody. Protein A may be measured down to 5 ng/ml in plasma and 0.5 ng/ml in buffer. The plasma samples were heat-inactivated before analysis and this eliminated interference in the assay caused by interaction of protein A with an excess of immunoglobulins. This assay provides a reliable and convenient method for the detection and quantitation of soluble protein A in human plasma. (Less)
Please use this url to cite or link to this publication:
author
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Protein A, ELISA, Plasma, human, Anti-protein A, Heat denaturation
in
Journal of Immunological Methods
volume
135
issue
1-2
pages
77 - 80
publisher
Elsevier
external identifiers
  • pmid:2273267
  • scopus:0025633213
ISSN
1872-7905
DOI
10.1016/0022-1759(90)90258-W
language
English
LU publication?
no
id
dd942e36-2f73-4cfd-b35d-22b374210092 (old id 1105128)
date added to LUP
2008-08-05 09:37:35
date last changed
2017-01-01 07:20:12
@article{dd942e36-2f73-4cfd-b35d-22b374210092,
  abstract     = {Quantitative determination of staphylococcal protein A in plasma is often hampered by the interaction between protein A and immunoglobulins. In human plasma, these interactions may not only involve the non-immune binding to the Fc or Fab regions of Ig but also antigen/antibody interaction by specific antibodies directed against protein A. In this paper we describe a method which can be used to quantitate nanogram amounts of protein A in the presence of human plasma. The ELISA used for the quantification of protein A is based on a double antibody solid-phase assay utilizing chicken anti-protein A as both capture and detector antibody. Protein A may be measured down to 5 ng/ml in plasma and 0.5 ng/ml in buffer. The plasma samples were heat-inactivated before analysis and this eliminated interference in the assay caused by interaction of protein A with an excess of immunoglobulins. This assay provides a reliable and convenient method for the detection and quantitation of soluble protein A in human plasma.},
  author       = {Nilsson, Rune and Davidsson, Bertil},
  issn         = {1872-7905},
  keyword      = {Protein A,ELISA,Plasma,human,Anti-protein A,Heat denaturation},
  language     = {eng},
  number       = {1-2},
  pages        = {77--80},
  publisher    = {Elsevier},
  series       = {Journal of Immunological Methods},
  title        = {Quantitation of protein A in human plasma is possible after heat inactivation of the samples},
  url          = {http://dx.doi.org/10.1016/0022-1759(90)90258-W},
  volume       = {135},
  year         = {1990},
}