A monoclonal antibody that specifically inhibits human salivary alpha-amylase.
Open Access
- 1 July 1987
- journal article
- research article
- Published by Oxford University Press (OUP) in Clinical Chemistry
- Vol. 33 (7) , 1158-1162
- https://doi.org/10.1093/clinchem/33.7.1158
Abstract
Our monoclonal antibody 88E8 specifically binds to and inhibits human salivary alpha-amylase (EC 3.2.1.1) and cross reacts negligibly with the pancreatic isoenzyme, inhibiting it by less than 1%, as compared with about 90% for the salivary isoenzyme. The antibody binds the S1 and S2 types of salivary alpha-amylase, but no pancreatic alpha-amylase isoenzyme forms. A pancreatic alpha-amylase assay involving 88E8 is under development, with alpha-glucosidase as auxiliary enzyme and p-nitrophenyl-maltoheptaoside as substrate; we give preliminary data on this assay. The assay has to be done by substrate start, because the antibody interacts very slowly with the enzyme in the presence of substrate. Assay results for pancreatic alpha-amylase correlate well with those for isoamylase assayed with use of an inhibitor from wheat-germ.This publication has 12 references indexed in Scilit:
- Rapid quantitative, specific measurement of pancreatic amylase in serum with use of a monoclonal antibody.Clinical Chemistry, 1985
- Preparation of Human Salivary σ-Amylase Specific Monoclonal AntibodyThe Journal of Biochemistry, 1985
- Sequences of cDNAs for human salivary and pancreatic α-amylasesGene, 1984
- Development of an agarose gel electrophoresis technique for determining alpha-amylase isoenzymes.Clinical Chemistry, 1984
- A new and rapid method for immunoglobulin class and subclass determination of mouse monoclonal antibodies using a solid-phase immunoradiometric assayJournal of Immunological Methods, 1984
- Serum α-amylase isozymes in mumps: estimation of salivary and pancreatic isozymes by isoelectric focusingClinica Chimica Acta; International Journal of Clinical Chemistry, 1981
- Isolation and characterization of four inhibitors from wheat flour which display differential inhibition specificities for human salivary and human pancreatic α-amylasesBiochimica et Biophysica Acta (BBA) - Enzymology, 1981
- Concentration of immunoreactive trypsin and activity of pancreatic isoamylase in serum compared in pancreatic diseases.Clinical Chemistry, 1980
- Tetranitromethane. A Reagent for the Nitration of Tyrosyl Residues in Proteins*Biochemistry, 1966
- The Determination of Enzyme Dissociation ConstantsJournal of the American Chemical Society, 1934