Studies on a trace cell lytic activity associated with alpha-lactalbumin.
alpha-Lactalbumin (alpha-LA) has been examined with a new and sensitive method for determination of lysozyme activity. Samples of bovine, human, equine, and rat alpha-LA exhibited cell lytic activity, from 2 X 10(-6) to 45 X 10(-6) of the specific activity of hen eggwhite lysozyme. The activity was chromatographically inseparable from bovine and human alpha-LA. Bovine serum albumin and purified beta-lactoglobulin were inactive. The pH profiles and reaction kinetics of bovine and human alpha-LA showed differences from those of the corresponding milk lysozymes, indicating that their lytic activities were not likely to have resulted from trace lysozyme content. Thus, it appears that a weak cell lytic activity is inherent to alpha-LA.
D000818:Animals; D001433:Bacteriolysis; D002417:Cattle; D006736:Horses; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D007768:Lactalbumin / Q000302:isolation & purification / Q000494:pharmacology*; D008837:Micrococcus / Q000187:drug effects; D008892:Milk / Q000201:enzymology*; D009113:Muramidase / Q000032:analysis; D051381:Rats; D013045:Species Specificity
D007768:Lactalbumin; D009113:Muramidase