The Molecular Structure of Fibrinogen^[*]

Abstract

Seminars in Thrombosis and Hemostasis (STH) celebrates 50 years of publishing in 2024. To celebrate this landmark event, STH is republishing some archival material. This manuscript represents the first full paper ever published in STH. The manuscript published without an abstract, and essentially covered in considerable detail the molecular structure of fibrinogen, as was known at that time. Fittingly, it covers some historical perspectives, the physicochemical properties and structure of fibrinogen across several species of animals (including humans) and its transformation into fibrin. We hope the readers of STH enjoy this journey into the past. This manuscript is accompanied by a Commentary that reflects on this past, as well as the journey towards contemporary understanding of the molecular structure of fibrinogen. As this is a republication of archival material, transformed into a modern format, we apologise in advance for any errors introduced during this transformation.

Keywords

fibrinogen - history - molecular structure - physicochemical properties - fibrin

^* The molecular weights of the three chain fragments[143] [148] were estimated at Aα/- = 6,000; Bβ)/- = 12,500; γ/- = 11,500. Therefore, in agreement with the figure of 58,000 obtained for intact (dimeric) N-DSK,[151] the minimum molecular weight for N-DSK (monomeric) is ∼29,000.

^** The Aα/-chain has alanine as the N-terminal residue, the A Yα/-chain variant is one amino acid residue shorter from the amino terminal (alanine is missing); the APα/-chain variant has the same sequence as Aα/-chain, except for residue number three, which is phosphoserine in place of serine; the AYPa/-chain variant has a serine phosphate in position 2 of the AYα/-chain. The slash (/) indicates degradation at a C-terminal position.

^* This article is a republished version of: Murano G. The molecular structure of Fibrinogen. Semin Thromb Hemost 1974;1:1–31

Publication History

Article published online:
24 November 2023

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