Antigenic assay for protein C determination in horses

Elizabeth G. Welles From the Department of Pathology, College of Veterinary Medicine, University of Georgia, Athens, GA 30602 (Welles, Prasse), the Department of Pathology, Grady Memorial Hospital, 80 Butler St, Atlanta, GA 30335 (Duncan), and the Enzyme Research Laboratories, South Bend, IN 46601 (Morris).

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Keith W. Prasse From the Department of Pathology, College of Veterinary Medicine, University of Georgia, Athens, GA 30602 (Welles, Prasse), the Department of Pathology, Grady Memorial Hospital, 80 Butler St, Atlanta, GA 30335 (Duncan), and the Enzyme Research Laboratories, South Bend, IN 46601 (Morris).

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Alexander Duncan From the Department of Pathology, College of Veterinary Medicine, University of Georgia, Athens, GA 30602 (Welles, Prasse), the Department of Pathology, Grady Memorial Hospital, 80 Butler St, Atlanta, GA 30335 (Duncan), and the Enzyme Research Laboratories, South Bend, IN 46601 (Morris).

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Michael J. Morris From the Department of Pathology, College of Veterinary Medicine, University of Georgia, Athens, GA 30602 (Welles, Prasse), the Department of Pathology, Grady Memorial Hospital, 80 Butler St, Atlanta, GA 30335 (Duncan), and the Enzyme Research Laboratories, South Bend, IN 46601 (Morris).

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SUMMARY

An antigenic assay was developed for determination of protein C in horses. Protein C, a natural, vitamin K-dependent anticoagulant component in blood, was isolated from equine plasma, a specific antibody was produced in goats, and a rocket electroimmunophoresis assay was established. Tests were performed to verify the identity of the isolated protein C and to determine the purity of the antibody. Protein C antigen was measured in plasma from 34 clinically normal horses, and values were compared with amidolytic function values. The mean (± sd) values for the 2 test methods were similar (antigen content, 104.5 ± 13.8%; amidolytic activity, 104.6 ± 17.5%), but the correlation coefficient was 0.1. Four horses given Na coumarin had markedly decreased plasma protein C amidolytic activity and minimal decrease in protein C antigen content.

SUMMARY

An antigenic assay was developed for determination of protein C in horses. Protein C, a natural, vitamin K-dependent anticoagulant component in blood, was isolated from equine plasma, a specific antibody was produced in goats, and a rocket electroimmunophoresis assay was established. Tests were performed to verify the identity of the isolated protein C and to determine the purity of the antibody. Protein C antigen was measured in plasma from 34 clinically normal horses, and values were compared with amidolytic function values. The mean (± sd) values for the 2 test methods were similar (antigen content, 104.5 ± 13.8%; amidolytic activity, 104.6 ± 17.5%), but the correlation coefficient was 0.1. Four horses given Na coumarin had markedly decreased plasma protein C amidolytic activity and minimal decrease in protein C antigen content.

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