A Comparative Study of Crosslinked and Noncrosslinked Fibrin from the Major Classes of Vertebrates

Martin L. Schwartz; Salvatore V. Pizzo; J Bolling Sullivan; Robert L. Hill; Patrick A. McKee

doi:10.1055/s-0038-1647774

Thrombosis and Haemostasis, Table of Contents

Thromb Haemost 1973; 29(02): 313-338
DOI: 10.1055/s-0038-1647774

Original Article

Schattauer GmbH

A Comparative Study of Crosslinked and Noncrosslinked Fibrin from the Major Classes of Vertebrates

Martin L. Schwartz

¹Department of Biochemistry, Duke University Medical Center, The Department of Medicine, Veterans Administration Hospital, Durham, North Carolina 27710, and the Duke University Marine Biology Laboratory, Beaufort, North Carolina

,

Salvatore V. Pizzo

¹Department of Biochemistry, Duke University Medical Center, The Department of Medicine, Veterans Administration Hospital, Durham, North Carolina 27710, and the Duke University Marine Biology Laboratory, Beaufort, North Carolina

,

J Bolling Sullivan

¹Department of Biochemistry, Duke University Medical Center, The Department of Medicine, Veterans Administration Hospital, Durham, North Carolina 27710, and the Duke University Marine Biology Laboratory, Beaufort, North Carolina

,

Robert L. Hill

¹Department of Biochemistry, Duke University Medical Center, The Department of Medicine, Veterans Administration Hospital, Durham, North Carolina 27710, and the Duke University Marine Biology Laboratory, Beaufort, North Carolina

,

Patrick A. McKee

¹Department of Biochemistry, Duke University Medical Center, The Department of Medicine, Veterans Administration Hospital, Durham, North Carolina 27710, and the Duke University Marine Biology Laboratory, Beaufort, North Carolina

› Author Affiliations

Abstract

Summary

Crosslinked and noncrosslinked fibrin formed by clotting whole plasma in the presence and absence of calcium has been examined by polyacrylamide gel electrophoresis in sodium dodecyl sulfate. The fibrin from 45 species of vertebrates with representatives from all classes except the Bradyodonti (Chimaeras) and a majority of the subclasses have been compared. Noncrosslinked fibrin from the mammals contained subunits resembling the α, β, and γ chains of human noncrosslinked fibrin. The molecular weight of the α-chains varied greatly, the molecular weight of the β-chains varied slightly, while the molecular weight of the γ-chains was apparently invariant. Nonerosslinked avian fibrins showed clearly resolved γ-chains with a molecular weight slightly smaller than human γ-chains. Avian α- and β-chains were usually not resolved. Nonerosslinked fibrin from the reptiles and amphibians contained a clearly resolved subunit with a molecular weight similar to that of human γ-chain. In crosslinked fibrin from all of the mammals, birds, reptiles, and amphibians the γ-chain was absent and a new band which corresponded to a dimer of the γ-chain was found, while high molecular weight polymers were only found in a few species. Fibrin formed from the plasma of the bony fishes was often difficult because of the problem of fibrinolysis ; however, non crosslinked fibrin from some species of bony fish had three clearly resolved subunits while the crosslinked fibrin from all of the species examined had dimers as the predominant crosslinked forms. The noncrosslinked fibrin from the cartilaginous fish had subunits in the same molecular weight range as the other vertebrate fibrins; however, the crosslinked fibrin was unique to this class because all of the fibrin subunits were involved in the crosslinking process. Dimers appeared to be a transient species, and a large number of different high molecular weight crosslinked species were formed. The crosslinked fibrin from the hagfish contained dimers and no higher molecular weight crosslinked forms. Rapid fibrinolysis complicated the interpretation of the results from all of the classes of fish.

Full Text

References

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