1962
DOI: 10.1159/000464763
|View full text |Cite
|
Sign up to set email alerts
|

Intravenous Administration of Human γ-Globulin

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
2

Citation Types

5
118
0
1

Year Published

1966
1966
2018
2018

Publication Types

Select...
8
1

Relationship

0
9

Authors

Journals

citations
Cited by 93 publications
(124 citation statements)
references
References 3 publications
(3 reference statements)
5
118
0
1
Order By: Relevance
“…Early IVIG preparations were produced from ISG by digestion with proteolytic enzymes to eliminate anticomplement activity. Anticomplement activity was believed to be the primary cause of adverse side-reactions when ISG was injected intravenously (Barandun et al 1962). The first commercial IVIG was produced by digestion of ISG with pepsin.…”
Section: Intravenous Immunoglobulin (Ivig)mentioning
confidence: 99%
See 1 more Smart Citation
“…Early IVIG preparations were produced from ISG by digestion with proteolytic enzymes to eliminate anticomplement activity. Anticomplement activity was believed to be the primary cause of adverse side-reactions when ISG was injected intravenously (Barandun et al 1962). The first commercial IVIG was produced by digestion of ISG with pepsin.…”
Section: Intravenous Immunoglobulin (Ivig)mentioning
confidence: 99%
“…Other early IVIG manufacturing procedures involved treatment of ISG with enzymes or with chemical reagents that reacted with amino acids located in the complement binding site (Barandun et al 1962;Sgouris 1967;Schroeder et al 1980). Unfortunately, each of these modifications reduced important antibody activities (Pollack 1983;Kim et al 1986;Bender and Hetherington 1987;Steele and Steele 1989) and shortened the half-lives of some antibodies (Janeway et al 1968;Winston et al 1982;Hagenbeek et al 1987Hagenbeek et al -1928.…”
Section: Intravenous Immunoglobulin (Ivig)mentioning
confidence: 99%
“…These heterogeneities include aggregation, fragmentation, deamidation, oxidation, N-and C-terminal differentiations. [2][3][4][5][6][7][8][9][10][11] Several analytical methods have been developed for these purposes, for example, SDS polyacrylamide gel electrophoresis for the determination of the purity of proteins, size exclusion chromatography for aggregation, ion exchange chromatography or hydrophobic interaction chromatography for the detection of deamidation and oxidation variants, and Ellman's assay for quantification of free thiol groups. 12,13 Capillary-based SDS electrophoresis (CE-SDS) is one version of the capillary gel electrophoresis (CGE) using soluble linear polymers.…”
Section: Introductionmentioning
confidence: 99%
“…Importantly, it was recognized that harsh chemical or enzymatic treatment of IgG may damage the molecule and reduce or abolish its natural function (1,18). A number of methods have now been developed for preparing gamma globulin for intravenous infusion, including chemical or enzyme treatment, acidification, and column chromatography.…”
Section: Introductionmentioning
confidence: 99%