Biochemical characterization and stability of immune globulin intravenous 10% liquid (Panzyga).

Panzyga is a new glycine-formulated immune globulin intravenous 10% liquid for the treatment of patients suffering from immunodeficiencies and autoimmune diseases. Panzyga is a high purity, native and functional IgG product with an IgG subclass distribution equivalent to normal plasma. The levels of hemagglutinins and accompanying plasma proteins (including IgA and IgM) are low.

Elevated Endotoxin Levels in Human Intravenous Immunoglobulin Concentrates Caused by (1->3)-{beta}-D-Glucans.

Unlabelled: Endotoxins have been measured routinely in the final product and during the production process to produce non-pyrogenic parenterals. Limulus-amoebocyte-lysate-reactive material was found in in-process samples and final product of one of Octapharma's intravenous immunoglobulin (IVIG) preparations. Limulus-amoebocyte-lysate (LAL) is activated by bacterial endotoxins and by (1→3)-β-D-glucans.

Anticomplementary activity of IVIG concentrates--important assay parameters and impact of IgG polymers.

Background And Objectives: A high concentration of large size polymers in intravenous immunoglobulin preparations was always correlated with high anticomplementary activity (ACA). In former days, high ACA was also linked to adverse reactions in patients. The goal of this study was to scrutinize critical parameters of the ACA assay and the influence of different polymer variants of IgG on the complement consumption.

Purification of intravenous immunoglobulin G from human plasma--aspects of yield and virus safety.

Plasma-derived intravenous immunoglobulin (IVIG) preparations have been successfully applied for the prophylactic prevention of infectious diseases in immunodeficient patients. In addition to its replacement therapy of primary and secondary antibody deficiencies, IVIG has found increased use in autoimmune and inflammatory diseases. IVIG has become the major plasma product on the global blood product market.

Isolation of esterified fatty acids bound to serum albumin purified from human plasma and characterised by MALDI mass spectrometry.

Human serum albumin (HSA) is the most abundant protein in plasma. It is known to transport drugs as well as endogenous ligands, like free fatty acids (FFA). A mass spectrometry based method was applied to analyze the albumin bound lipid ligands.