Please use this identifier to cite or link to this item: http://ahro.austin.org.au/austinjspui/handle/1/13312
Title: Studies to demonstrate inhibition of functional activity of neutrophil lysosomal enzymes with ANCA.
Authors: Chang, L;Savige, Judy A
Affiliation: Department of Haematology, Heidelberg Repatriation Hospital Victoria, Australia.
Issue Date: 16-May-1993
Citation: Advances in Experimental Medicine and Biology; 336(): 97-100
Abstract: Many autoantibodies that have enzymes as their targets bind to the catalytic sites and inhibit enzymatic activity. We have established functional assays for the targets of anti-neutrophil cytoplasm antibodies (ANCA) in order to determine whether these antibodies are directed against the corresponding catalytic sites. Anti-proteinase 3 activity was measured by the cleavage of alpha-naphthyl acetate; myeloperoxidase activity by peroxidation of monochlorodimedon or guaiacol using hydrogen peroxide; and elastase activity by a fluorimetric assay of the hydrolytic product of N-succ (ala)3 amido-methyl coumarin. The addition of immunoglobulin from patients with ANCA to these assays did not result in inhibition of functional activity of the corresponding enzyme when compared with normal immunoglobulin. Furthermore the removal of specific immunoglobulin by solid phase adsorption to the corresponding antigen did not result in an increase in enzymatic activity compared with the starting material. However preliminary results suggest that anti-neutrophil proteinase 3 binding may be inhibited in a solid-phase ELISA by preincubation with a peptide corresponding to the catalytic site.
Internal ID Number: 8296682
URI: http://ahro.austin.org.au/austinjspui/handle/1/13312
URL: http://www.ncbi.nlm.nih.gov/pubmed/8296682
Type: Journal Article
Subjects: Antibodies, Antineutrophil Cytoplasmic
Autoantibodies.pharmacology
Binding Sites
Humans
Immunoglobulin G.pharmacology
Lysosomes.enzymology
Myeloblastin
Neutrophils.enzymology
Pancreatic Elastase.antagonists & inhibitors
Peroxidase.antagonists & inhibitors
Protease Inhibitors.pharmacology
Serine Endopeptidases.metabolism
Appears in Collections:Journal articles

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