A V region-connected autoreactive subfraction of normal human serum immunoglobulin G

1992 ◽  
Vol 22 (7) ◽  
pp. 1701-1706 ◽  
Author(s):  
Gilles Dietrich ◽  
Srinivas-Venkatesh Kaveri ◽  
Michel D. Kazatchkine
Keyword(s):  
Human Serum ◽  
Immunoglobulin G ◽  
Normal Human Serum ◽  
Serum Immunoglobulin ◽  
Normal Human ◽  
V Region

scholarly journals Mannan-Specific Immunoglobulin G Antibodies in Normal Human Serum Accelerate Binding of C3 to Candida albicans via the Alternative Complement Pathway

1998 ◽  
Vol 66 (10) ◽  
pp. 4845-4850 ◽  
Author(s):  
Mason X. Zhang ◽  
Thomas R. Kozel
Keyword(s):  
Candida Albicans ◽  
Human Serum ◽  
Immunoglobulin G ◽  
Alternative Pathway ◽  
Normal Human Serum ◽  
Yeast Cells ◽  
Classical Pathway ◽  
Intact Antibody ◽  
Alternative Complement ◽  
Normal Human

ABSTRACT Candida albicans activates the classical and alternative complement pathways, leading to deposition of opsonic complement fragments on the cell surface. Our previous studies found that antimannan immunoglobulin G (IgG) in normal human serum (NHS) allows C. albicans to initiate the classical pathway. The purpose of this study was to determine whether antimannan IgG also plays a role in initiation of the alternative pathway. Pooled NHS was rendered free of classical pathway activity by chelation of serum Ca2+ with EGTA alone or in combination with immunoaffinity removal of antimannan antibodies. Kinetic analysis revealed a 6-min lag in detection of C3 binding to C. albicans incubated in EGTA-chelated NHS, compared to a 12-min lag in NHS that was both EGTA chelated and mannan absorbed. The 12-min lag was shortened to 6 min by addition of affinity-purified antimannan IgG. The accelerating effect of antimannan IgG on alternative pathway initiation was dose dependent and was reproduced in a complement binding reaction consisting of six purified proteins of the alternative pathway. Both Fab and F(ab′)2 fragments of antimannan IgG facilitated alternative pathway initiation in a manner similar to that observed with intact antibody. Immunofluorescence analysis showed that addition of antimannan IgG to EGTA-chelated and mannan-absorbed serum promoted an early deposition of C3 molecules on the yeast cells but had little or no effect on distribution of the cellular sites for C3 activation. Thus, antimannan IgG antibodies play an important regulatory role in interactions between the host complement system and C. albicans.

scholarly journals Neutrophil attractant protein-1-immunoglobulin G immune complexes and free anti-NAP-1 antibody in normal human serum.

1992 ◽  
Vol 90 (2) ◽  
pp. 471-481 ◽  
Author(s):  
I Sylvester ◽  
T Yoshimura ◽  
M Sticherling ◽  
J M Schröder ◽  
M Ceska ◽  
...  
Keyword(s):  
Human Serum ◽  
Immunoglobulin G ◽  
Immune Complexes ◽  
Normal Human Serum ◽  
Normal Human

Evaluation of a commercially available radioimmunoassay kit for measurement of doxorubicin in plasma.

1982 ◽  
Vol 28 (1) ◽  
pp. 119-121 ◽  
Author(s):  
E Piall ◽  
G W Aherne ◽  
V Marks
Keyword(s):  
Human Serum ◽  
Normal Human Serum ◽  
Nonspecific Effects ◽  
Normal Human ◽  
Doxorubicin Concentration

Abstract We evaluated a commercially available (Diagnostic Biochemistry Inc.) doxorubicin 125I radioimmunoassay kit. This kit gave a high apparent doxorubicin concentration (greater than 12 micrograms/L), which was not linearly related to dilution, for two pools of normal human serum and plasma and also for samples collected from patients before they received the drug. In contrast, a doxorubicin 3H radioimmunoassay developed by us gave a low blank (2 micrograms/L), which was linearly related to dilution, for the same pools and patients' samples. Doxorubicin concentrations in the plasma of patients receiving the drug were compared by the two methods; the kit gave results five- to 10-fold those obtained with our assay. High nonspecific interference by serum and plasma as measured by the 125I radioimmunoassay must therefore be borne in mind by users of the kit, and we suggest that results should be corrected for these nonspecific effects.

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