scholarly journals Development of a Human-Murine Chimeric Immunoglobulin M for Use in the Serological Detection of Human Alphavirus Antibodies

2011 ◽  
Vol 18 (12) ◽  
pp. 2181-2182 ◽  
Author(s):  
Brett A. Thibodeaux ◽  
Nathan M. Liss ◽  
Amanda N. Panella ◽  
John T. Roehrig
Keyword(s):  
Monoclonal Antibody ◽  
Immunosorbent Assay ◽  
Immunoglobulin M ◽  
Murine Monoclonal Antibody ◽  
Enzyme Linked Immunosorbent Assay ◽  
Serological Detection ◽  
Antibody Capture

ABSTRACTDiagnosis of human alphaviral infections relies on serological techniques, such as the immunoglobulin M antibody capture–enzyme-linked immunosorbent assay (MAC-ELISA). We have humanized the alphavirus broadly cross-reactive murine monoclonal antibody 1A4B-6 to create a reagent capable of replacing human positive sera in the MAC-ELISA for diagnosis of human alphaviral infections.

A Murine Monoclonal Antibody Based Enzyme-Linked Immunosorbent Assay for Almond (Prunus dulcis L.) Detection

2013 ◽  
Vol 61 (45) ◽  
pp. 10823-10833 ◽  
Author(s):  
Mengna Su ◽  
Mahesh Venkatachalam ◽  
Changqi Liu ◽  
Ying Zhang ◽  
Kenneth H. Roux ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Immunosorbent Assay ◽  
Prunus Dulcis ◽  
Murine Monoclonal Antibody ◽  
Enzyme Linked Immunosorbent Assay

scholarly journals Characterization of a Monoclonal Antibody That Binds to an Epitope on Soluble Bacterial Peptidoglycan Fragments

2001 ◽  
Vol 8 (3) ◽  
pp. 647-651 ◽  
Author(s):  
Glenn J. Merkel ◽  
Barbara A. Scofield
Keyword(s):  
Staphylococcus Aureus ◽  
Monoclonal Antibody ◽  
Immunosorbent Assay ◽  
Enzymatic Digestion ◽  
Immunoglobulin M ◽  
Enzyme Linked Immunosorbent Assay ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Bacterial Peptidoglycan

ABSTRACT We employed an inhibition-type enzyme-linked immunosorbent assay (ELISA) to characterize a murine immunoglobulin M monoclonal antibody (MAb) that bound soluble macromolecular peptidoglycan (PG). With this ELISA, the MAb was capable of detecting soluble PG concentrations of less than 10 ng/ml. Enzymatic digestion of PG reduced binding by more than 100-fold, implying that the epitope recognized by this antibody depended on repeating subunits within the glycan backbone. Additionally, the MAb bound to epitopes on both O-acetylated and non-O-acetylated PG fragments from gram-negative bacteria, as well as PG fragments from Staphylococcus aureus and PG fragments released into the medium by a number of gram-positive and gram-negative bacteria.

scholarly journals Measurement of free, one-chain tissue-type plasminogen activator in human plasma with an enzyme-linked immunosorbent assay based on an active site-specific murine monoclonal antibody

Blood ◽  
1987 ◽  
Vol 69 (1) ◽  
pp. 284-289 ◽  
Author(s):  
P Holvoet ◽  
J Boes ◽  
D Collen
Keyword(s):  
Monoclonal Antibody ◽  
Plasminogen Activator ◽  
Immunosorbent Assay ◽  
Active Site ◽  
Venous Occlusion ◽  
Murine Monoclonal Antibody ◽  
Tissue Type ◽  
Enzyme Linked Immunosorbent Assay ◽  
Tissue Type Plasminogen Activator ◽  
Type Plasminogen Activator

Abstract An enzyme-linked immunosorbent assay for free tissue-type plasminogen activator (t-PA) in human blood was developed based on a murine monoclonal antibody directed against the active site of t-PA. The lower limit of sensitivity of the assay applied to plasma is 2 ng/mL for one- chain t-PA but only 100 ng/mL for two-chain t-PA. Free t-PA in plasma taken at rest was found in 6 of 21 healthy subjects (4.5 +/- 0.8 ng/mL, mean +/- SD) and increased to 14 +/- 7.0 ng/mL after venous occlusion in 18 of these individuals. A linear correlation between total t-PA and free t-PA was observed with r = 0.92 (n = 18) and a slope of 1.08, indicating that t-PA released from the vessel wall circulates in the blood as the one-chain form. In 16 of 18 patients with deep vein thrombosis, the increase of total t-PA antigen after venous occlusion was comparable to that observed in controls, but the free t-PA was significantly lower or undetectable. The present assay for free t-PA may be useful for the investigation of the release and inhibition of t- PA under physiological, pharmacological, or pathological conditions in humans.

scholarly journals Measurement of free, one-chain tissue-type plasminogen activator in human plasma with an enzyme-linked immunosorbent assay based on an active site-specific murine monoclonal antibody

Blood ◽  
1987 ◽  
Vol 69 (1) ◽  
pp. 284-289
Author(s):  
P Holvoet ◽  
J Boes ◽  
D Collen
Keyword(s):  
Monoclonal Antibody ◽  
Plasminogen Activator ◽  
Immunosorbent Assay ◽  
Active Site ◽  
Venous Occlusion ◽  
Murine Monoclonal Antibody ◽  
Tissue Type ◽  
Enzyme Linked Immunosorbent Assay ◽  
Tissue Type Plasminogen Activator ◽  
Type Plasminogen Activator

An enzyme-linked immunosorbent assay for free tissue-type plasminogen activator (t-PA) in human blood was developed based on a murine monoclonal antibody directed against the active site of t-PA. The lower limit of sensitivity of the assay applied to plasma is 2 ng/mL for one- chain t-PA but only 100 ng/mL for two-chain t-PA. Free t-PA in plasma taken at rest was found in 6 of 21 healthy subjects (4.5 +/- 0.8 ng/mL, mean +/- SD) and increased to 14 +/- 7.0 ng/mL after venous occlusion in 18 of these individuals. A linear correlation between total t-PA and free t-PA was observed with r = 0.92 (n = 18) and a slope of 1.08, indicating that t-PA released from the vessel wall circulates in the blood as the one-chain form. In 16 of 18 patients with deep vein thrombosis, the increase of total t-PA antigen after venous occlusion was comparable to that observed in controls, but the free t-PA was significantly lower or undetectable. The present assay for free t-PA may be useful for the investigation of the release and inhibition of t- PA under physiological, pharmacological, or pathological conditions in humans.

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