Open AccessFibrinogen heterogeneity in horses
Author(s) -
Russell Elise B.,
Courtman Natalie F.,
Santos Leilani L.,
TennentBrown Brett S.
Publication year - 2021
Publication title -
journal of veterinary internal medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.356
H-Index - 103
eISSN - 1939-1676
pISSN - 0891-6640
DOI - 10.1111/jvim.16065
Subject(s) - fibrinogen , horse , blot , microbiology and biotechnology , antiserum , polyacrylamide gel electrophoresis , molecular mass , blood proteins , medicine , chromatography , biochemistry , biology , chemistry , immunology , antibody , enzyme , gene , paleontology
Background Fibrinogen heterogeneity has been observed in humans and can influence fibrinogen measurements when using the modified Clauss assay. We hypothesized that fibrinogen heterogeneity also exists in horses. Objectives To determine whether fibrinogen heterogeneity exists in horses. Animals Five clinically healthy horses from the university equine teaching herd. Methods Presumed fibrinogen was purified from pooled citrated plasma and electrophoresis performed. The purified protein was subjected to Western blotting using sheep antiserum against human fibrinogen, and liquid chromatography‐tandem mass spectrometry (LC‐MS/MS). Results Gel electrophoresis of nonreduced equine purified protein yielded 2 protein bands (approximately 377 and 318 kDa) that corresponded with the molecular weights of human high molecular weight fibrinogen and low molecular weight fibrinogen fractions, respectively. Electrophoretograms of reduced purified protein, Western blots, and LC‐MS/MS supported that the purified nonreduced protein bands were fibrinogen. Conclusion Fibrinogen heterogeneity exists in horses.