This assay employs a two-site sandwich ELISA to quantitate LZM in samples. An antibody specific for LZM has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and any LZM present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for LZM is added to the wells. After washing, Streptavidin conjugated Horseradish Peroxidase (HRP) is added to the wells. Following a wash to remove any unbound avidin-enzyme reagent, a substrate solution is added to the wells and color develops in proportion to the amount of LZM bound in the initial step. The color development is stopped and the intensity of the color is measured.
 

Lysozyme, also known as muramidase or N-acetylmuramide glycanhydrolase, are a family of enzymes (EC 3.2.1.17) which damage bacterial cell walls by catalyzing hydrolysis of 1,5-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. Lysozyme is abundant in a number of secretions, such as tears, saliva, human milk and mucus. It is also present in cytoplasmic granules of the polymorphonuclear neutrophils (PMN). Large amounts of lysozyme can be found in egg white. C-type lysozymes are closely related to alpha-lactalbumin in sequence and structure making them part of the same family.