Tolerance of Scottish National Blood Transfusion Service Intravenous Immunoglobulin in Patients with Primary Hypogammaglobulinaemia: Report of 1235 Infusions

A total of 1235 immunoglobulin infusions were carried out as replacement therapy in 37 patients suffering from primary hypogammaglobulinemia from 1983 to 1987, using Scottish National Blood Transfusion Service (SNBTS) IV IgG, manufactured by cold ethanol fractionation of plasma, ultrafiltration and mild pepsin proteolysis at pH4. Ten patients experienced adverse reactions during 34 infusions (2.8% of all infusions) and all but five were mild; 21 (62%) of the adverse reactions were encountered in the patients' first five infusions. A maximum immunoglobulin infusion rate of 5 mg/kg/min was tolerated without adverse reaction.

Functional Relationship of Polymerization Sites of Vertebrate Fibrinogens

Various studies on the interaction of immobilized mammalian fibrinogen and fibrin monomers with some fibrinogen derivatives demonstrated the presence of two sets of polymerization sites in the mammalian fibrinogen molecule. We obtained the same results while investigating the fibrinogen molecules of other classes of vertebrates /Pisces. Amphibia. Aves/. Despite significant differences among their subunit structures, all of them contain polymerization sites homologous to mammalian counterparts. Moreover, due to great functional similarity, fibrinogen or fibrin monomers of the analyzed species of Pisces. Amphibia. Aves and Mammalia interacted in a specific way with immobilized pig fibrin monomers or fibrinogen, respectively. Using these pig affinity adsorbents, fibrinogen and fibrin monomers of different vertebrates were isolated directly from plasma and analyzed by SDS polyacrylamide gel electrophoresis. Polypeptide compositions of eluted proteins were identical to those obtained for corresponding fibrinogen preparations isolated by cold-ethanol fractionation method. It appears to indicate that the nature of polymerization sites in vertebrate fibrinogens is alike.

Functional Relationship of Polymerization Sites of Vertebrate Fibrinogens

Various studies on the interaction of immobilized mammalian fibrinogen and fibrin monomers with some fibrinogen derivatives demonstrated the presence of two sets of polymerisation sites In the mammalian fibrinogen molecule. We obtained the same results while investigating the fibrinogen molecules of other classes of vertebrates /Pisces, Amphibia, Aves/. Despite significant differences among their subunit structures, all of them contain polymerization sites homologous to mammalian counterparts. Moreover, due to great functional similarity, fibrinogen or fibrin monomers of the analyzed species of Pisces, Amphibia, Ayes and Mammalia interacted in a specific way with Immobilized pig fibrin monomers or fibrinogen, respectively. Using these pig affinity adsorbents, fibrinogen and fibrin monomers of different vertebrates were isolated directly from plasma and analyzed by SDS Polyacrylamide gel electrophoresis. Polypeptide compositions of eluted proteins were identical to those obtained for corresponding fibrinogen preparations isolated by cold-ethanol fractionation method. It appears to indicate that the nature of polymerization sites in vertebrate fibrinogens is alike.