The cold-insoluble globulin of human plasma. I. Purification, primary characterization, and relationship to fibrinogen and other cold-insoluble fraction components.

A cell-type specific glycoprotein antigen (SFA) from fibroblast surface appears in human plasma and serum. The amount of SFA in serum was reduced if the blood coagulation clot was removed at a low temperature. SFA could be bound to Sepharose-conjugated fibrinogen and to fibrin powder at 0 degrees C and was subsequently released when the temperature was elevated to plus 37 degrees C. This procedure resulted in a 10-fold enrichment of SFA relative to other serum proteins. SFA was found to be concentrated in the cryoprecipitate fraction of human plasma and was copurified with the cold insoluble globulin (CIG) with procedures published for the purification of the latter component. SFA/CIG is not soluble at low temperatures as such and its appearance in the cryoprecipitate fraction of plasma is likely to be due to its affinity to cryofibrinogen evident from these experiments. The biological significance of the interaction of fibroblast surface SFA moleculres with fibrin(ogen) is not known.

/pdf/interaction-of-soluble-fibroblast-surface-antigen-with-35jm15klc8.pdf

Interaction of soluble fibroblast surface antigen with fribrinogen and fibrin.

Publisher Summary The thrombin-induced conversion of fibrinogen to fibrin that is the primary subject of this review is essentially the final stage in the complex series of processes involved in blood coagulation. Fibrinogen exists in normal blood, while thrombin is present as its precursor prothrombin. The coagulation process consists of the conversion of prothrombin to thrombin and of the subsequent action of thrombin on fibrinogen to produce fibrin. In the fibrinogen-fibrin conversion fibrinogen, already a high polymer of many amino acids is converted to an even higher polymeric form or coagulum, the fibrin clot. Prothrombin can be converted to thrombin in a series of highly complex, and as yet not well understood, reactions. The chapter explores four of the processes by which the conversion of prothrombin to thrombin takes place. These are (1) activation by citrate, (2) activation by calcium ions, Ac-globulin and thromboplastin, (3) activation by calcium ions, platelets and thromboplastin, and (4) activation by trypsin. The chapter concludes by addressing the various problems of current interest in protein chemistry, which appear in the study of the fibrinogen-fibrin conversion. The first step is an example of a limited proteolysis by a protease of curious specificity. This proteolysis may turn out to be one of the first illustrations of the existence of “strong” peptide bonds in proteins. Further, it offers a nice illustration of the phenomenon of unmasking or activation in biological systems. The second step involves protein-protein associations with unequal association constants. The last step may involve gel formation or crystallization.

The Fibrinogen-Fibrin Conversion1

Complex carbohydrates of the extracellular matrix structures, interactions and biological roles.

The concentrations of 22 proteins were determined on plasma from normal men and women, from pregnant women and from newborns. Most values were given not in absolute units, but relative to those of a reference plasma pool. The variations with sex found and the relative values found in pregnant women and newborns agreed with data reported by others. The values found for 14 major proteins were studied for any intercorrelations. Five proteins, haptoglobin, fibrinogen, orosomucoid, β1C-globulin and β1E-globulin, all known as “acute phase reactants”, were fairly closely correlated. In some respects hemopexin, ceruloplasmin and plasminogen seemed to be associated to this group in different ways, while another protein, a,-antitrypsin, usually also classified an an “acute phase reactant”, seemed not to belong to this group.

Variation of the concentrations of some plasma proteins in normal adults, in pregnant women and in newborns.

The Non-clotting Component of the Human Plasma Fraction I-1 (“Cold Insoluble Globulin”)1

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The Non-clotting Component of the Human Plasma Fraction I-1 (“Cold Insoluble Globulin”)1