ArticleSnyder JA, Harrison JH.
J Exp Zool. 1977 Oct;202(1):89-96.
Frog Lysozyme has been purified by sequential application of acid extraction, salt fractionation, CM-cellulose chromatography, heat treatment, and gel filtration. Eight isozymes of purified lysozyme were found to be stable during prolonged storage. Isozymes were separated by preparative polyacrylamide gel electrophoresis, Ninety percent of the lytic activity of frog ovarian egg was represented by forms 7 and 8, the most highly charged isozymes. Seventy-eight percent of frog liver lysozyme activity was that of form 4. Forms 7 and 8 differed from form 4 by being larger (apparent molecular weight of 18,000 vs. 16,000), by remaining active in more acidic environment, and by exhibiting a dependency upon NaCl for activity. Antiserum prepared against frog form 4 did not react with frog forms 7 and 8 and antiserum to chicken egg-white lysozyme did not react with any frog lysozymes. All frog lysozymes showed identical reversible binding to deaminated chitin. Apparent size differences and lack of immunological cross-reactivity suggest that at least some of the isozymes are non-allelic.