title: Some properties of the lysozymes in serum and colostrum from cows with high and low lytic power against Micrococcus lysodeikticus.
abstract: Previous work has uncovered a dominant gene for high bacteriolytic activity of bovine serum against the test bacterium Micrococcus lysodeikticus. This major gene effect is also fully expressed in colostrum. In the present study the lytic power of serum and colostral whey from high and low level cows was subjected to a degree of characterization. It was found that the enzyme activities studied exhibited properties in accordance with those defined for a lysozyme (EC 3.2.1.17), i.e. (1) lysis of a suspension of M. lysodeikticus, (2) basic protein (pI = 10.0 and pI = 10.3 for bovine serum lysozyme (BSL) and bovine colostrum lysozyme (BCL), respectively), (3) molecular weight (MW) approximately 16 000 for both BSL and BCL, (4) liberation of free reducing sugars during action on cell wall peptidoglycan (the kinetics of BSL and BCL differed strongly), and (5) fairly heat stable, especially at acidic pH and relative labile at alkaline pH (BCL was far more sensitive to heating at alkaline pH than was BSL). The dramatic differences in activity between high and low level animals might be due to a major genetic mechanism influencing the amount of, or the activity of, circulating enzyme molecules, rather than a structural gene coding for a certain enzyme with a particular specific activity. This is also supported by the high correlation between the lytic capacity of BSL and BCL in spite of the different properties of these lysozymes (i.e. in respect of pI, enzyme kinetics and heat stability) reported in the present study.
mesh_terms: D000818:Animals; D002417:Cattle; D003126:Colostrum / Q000201:enzymology*; D005260:Female; D005796:Genes; D007700:Kinetics; D008837:Micrococcus / Q000254:growth & development*; D008970:Molecular Weight; D009113:Muramidase / Q000097:blood / Q000235:genetics / Q000378:metabolism*; D011247:Pregnancy; D013045:Species Specificity
chemical_list: D009113:Muramidase