Assessment of Peptidylarginine Deiminase Activity by ELISA Using Human Fibrinogen as Substrate

Dres Damgaard; Claus H Nielsen

doi:10.1007/978-1-4939-8949-2_20

Assessment of Peptidylarginine Deiminase Activity by ELISA Using Human Fibrinogen as Substrate

Methods Mol Biol. 2019:1901:239-242. doi: 10.1007/978-1-4939-8949-2_20.

Authors

Dres Damgaard^{1

2}, Claus H Nielsen^{3

4}

Affiliations

¹ Institute for Inflammation Research, Center for Rheumatology and Spine Diseases, Copenhagen University Hospital, Rigshospitalet, Copenhagen, Denmark. dres.damg@gmail.com.
² Section for Periodontology, Microbiology and Community Dentistry, Department of Odontology, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark. dres.damg@gmail.com.
³ Institute for Inflammation Research, Center for Rheumatology and Spine Diseases, Copenhagen University Hospital, Rigshospitalet, Copenhagen, Denmark.
⁴ Section for Periodontology, Microbiology and Community Dentistry, Department of Odontology, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.

PMID: 30539583
DOI: 10.1007/978-1-4939-8949-2_20

Abstract

An enzyme-linked immunosorbent assay (ELISA) for measurement of the activity of peptidylarginine deiminases (PADs), the enzymes responsible for citrullination, is described. It uses fibrinogen as substrate for the enzyme and a commercial antibody specific for the citrullinated form of fibrinogen.

Keywords: Citrullination; ELISA; Fibrinogen; Peptidylarginine deiminase; Rheumatoid arthritis.

MeSH terms

Enzyme Assays
Enzyme-Linked Immunosorbent Assay / methods*
Fibrinogen / metabolism*
Humans
Protein-Arginine Deiminases / metabolism*
Substrate Specificity

Substances

Fibrinogen
Protein-Arginine Deiminases