Purification and characterization of two lysozymes from rainbow trout (Salmo gairdneri).
1. Two different lysozymes, designated I and II, were purified from the kidney of rainbow trout. The enzymes had isoelectric points of approximately 9.5 and 9.65, and differed in their binding characteristics to a cation exchanger. Lysozyme II had the highest specific activity against Micrococcus luteus. 2. By sodium dodecyl sulphate gel electrophoresis, a molecular mass of 14.4 kDa was established for the two lysozymes. 3. For both type I and II enzymes, optimum pH under the present conditions was 5.5 and optimum temperature (at pH 6.2) around 45 degrees C. 4. N-terminal amino acid sequence determination indicated that the two trout lysozymes were c-type lysozymes. 5. The fish lysozymes had a much higher rate of diffusion in agar than did the other lysozymes tested (possibly due to less interaction with agarose). This implies that a foreign lysozyme, such as hen egg white lysozyme, should not be used as a standard when assaying lysozyme activity with the lysoplate technique.
Grinde
B
B
Department of Animal Husbandry and Genetics, Norwegian College of Veterinary Medicine, Oslo.
Jollès
J
J
Jollès
P
P
D000595:Amino Acid Sequence; D000818:Animals; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D007668:Kidney / Q000201:enzymology; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009113:Muramidase / Q000145:classification / Q000302:isolation & purification*; D012487:Salmonidae / Q000378:metabolism*; D013696:Temperature; D014337:Trout / Q000378:metabolism*
D009113:Muramidase