Feline and canine milk lysozymes.
1. The electrophoretic characteristics of feline (Felis catus) and canine (Canis familiaris) milk lysozymes were studied using starch gel electrophoresis and isoelectric focusing. 2. Feline milk lysozyme was found to be polymorphic (two variants, designated A and B with frequencies of 0.13 and 0.87, respectively). Canine milk lysozyme was not polymorphic. 3. The lytic activities of feline and canine milk lysozymes were examined in buffers of varying pH and ionic strength. Preliminary kinetics studies were done. 4. Maximal lytic activity for both lysozymes was found in imidazole-HCl buffer pH 7.4 and both exhibited second order reaction kinetics. 5. Amino acid compositions of both lysozymes were determined.
Halliday
J A
JA
Australian Equine Blood Typing Research Laboratory, Department of Physiology and Pharmacology, University of Queensland, St. Lucia, Brisbane.
Bell
K
K
Shaw
D C
DC
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002415:Cats; D004285:Dogs; D004592:Electrophoresis, Starch Gel; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D007700:Kinetics; D008892:Milk / Q000201:enzymology*; D009113:Muramidase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*
D000596:Amino Acids; D009113:Muramidase