Enzyme-Linked Immunosorbent Assay of Autoantibodies against Mitochondrial Glycerophosphate Dehydrogenase in Insulin-Dependent and Non-Insulin-Dependent Diabetic Subjects

1997 ◽  
Vol 62 (2) ◽  
pp. 172-177 ◽  
Author(s):  
M.E. Fabregat ◽  
C. Benito ◽  
M. Gudayol ◽  
J. Vidal ◽  
T. Gallart ◽  
...  
Keyword(s):  
Immunosorbent Assay ◽  
Enzyme Linked Immunosorbent Assay ◽  
Glycerophosphate Dehydrogenase ◽  
Insulin Dependent ◽  
Insulin Dependent Diabetic

Profile of Renal Permselectivity by Simultaneous Enzyme-Linked Immunosorbent Assay of Albumin, Transferrin, IgG, and α1-Microglobulin with a New Microplate Reader

1992 ◽  
Vol 38 (5) ◽  
pp. 636-641 ◽  
Author(s):  
R A Magnotti ◽  
J P Eberly ◽  
P R Khoury ◽  
S R Daniels ◽  
D J Drozda ◽  
...  
Keyword(s):  
Immunosorbent Assay ◽  
Light Emitting Diode ◽  
Normal Subjects ◽  
Insulin Dependent Diabetes Mellitus ◽  
Dependent Diabetes Mellitus ◽  
Enzyme Linked Immunosorbent Assay ◽  
Healthy Children ◽  
Light Emitting ◽  
Insulin Dependent ◽  
Excretion Rates

Abstract A competitive enzyme-linked immunosorbent assay (ELISA) is described for determining a renal permselectivity profile involving the urinary proteins albumin, transferrin, IgG, and alpha 1-microglobulin (alpha 1-m). The ELISA reader uses a computer-controlled array of multiplexed light-emitting diode (LED)-photodiode pairs for rapid measurements of absorbance on microplates. A 3,3'-dimethylnaphthidine reagent adapts the 3,5,3',5'-tetramethylbenzidine chromophore to monochromatic LED emission at 550 nm. We applied this ELISA to the determination of renal permselectivity in healthy children and young adults and in children with insulin-dependent diabetes mellitus. The geometric means (and SD) of protein excretion rates in a group of 85 normal subjects were as follows: albumin, 3.5 micrograms/min (1.83); transferrin, 173 ng/min (2.76); IgG, 1.11 micrograms/min (2.22), and alpha 1-m, 0.98 microgram/min (2.36).

Plasminogen Interactions with Immobilized Fibrinogen

1989 ◽  
Vol 62 (04) ◽  
pp. 1078-1082 ◽  
Author(s):  
Burt Adelman ◽  
Patricia Ouynn
Keyword(s):  
Immunosorbent Assay ◽  
Aminocaproic Acid ◽  
Enzyme Linked Immunosorbent Assay ◽  
Binding Regions ◽  
Dose Dependent Fashion ◽  
Epsilon Aminocaproic Acid ◽  
Dose Dependent

SummaryThis report describes the binding of plasminogen to fibrinogen adsorbed onto polystyrene wells. Binding was determined by enzyme linked immunosorbent assay. Both glu- and lys-plasminogen bound to immobilized fibrinogen in a dose-dependent fashion. However, more lys- than glu-plasminogen bound when equal concentrations of either were added to immobilized fibrinogen. Plasminogen binding was inhibited by epsilon aminocaproic acid indicating that binding was mediated via lysine-binding regions of plasminogen. Soluble fibrinogen added in excess of immobilized fibrinogen did not compete for plasminogen binding but fibrinogen fragments produced by plasmin digestion of fibrinogen did. Treatment of immobilized fibrinogen with thrombin caused a small but significant (p <0.01) increase in plasminogen binding. These studies demonstrate that immobilized fibrinogen binds both glu- and lys-plasminogen and that binding is mediated via lysine-binding regions. These interactions may facilitate plasminogen binding to fibrinogen adsorbed on to surfaces and to cells such as platelets which bind fibrinogen.

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