Abstract
The bacteriolytic enzyme lysozyme has been shown to depolymerize and hydrolyze a mucopolysaccharide obtained from lysozyme-susceptible organisms. 1 The depolymerization of this substrate as measured viscosimetrically has been used as an accurate and speedy test for the assay of the enzyme.
Acetone desiccated mucosa of horse and hog stomachs were found by this method to contain 15.2 and 714 units of lysozyme per gram respectively (samples were obtained through the courtesy of Dr. R. H. Barnes of Sharp and Dohme, Philadelphia). Mucosa of the fundus, antrum, pylorus and duodenum of human stomachs resected for peptic ulcer were found to contain mean lysozyme titers of 12, 120, 316, and 213 units per gram of wet weight respectively. One case of ulcer of the duodenum showed the following lysozyme titers: fundus: 2, antrum: 200, pylorus: 224, and duodenum: 400 units per gram.
Assays of the gastric juice of 30 normal individuals and 29 unoperated ulcer cases showed mean lysozyme values of 7.69 and 14.3 units per cc respectively. The difference of the means is statistically significant. All cases with obstruction, as evidenced by intractable vomiting, had a mean lysozyme titer of 1.7 units per cc. This low value is probably explained by peptic destruction of lysozyme. Approximately 50 γ of crystalline pepsin inactivated (at 37°C) 81% of an equivalent amount of lysozyme in one hour and 92% in 2 hours. The mean lysozyme titers of the unoperated ulcer cases without the 7 obstructed individuals was 18.3 units
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