The temperature and pH-dependent transition of hen lysozyme. Characterization of two temperature-defined domains and of an N-acetylglucosamine (inhibitor)-insensitive form.
The previously described temperature and pH-dependent transition in the solid state of hen lysozyme was studied in solution. Experiment concerning the velocity of lysis of M. luteus by lysozyme and its behavior in presence of an inhibitor (GlcNAc) as well as a reinvestigation of the Arrhenius curves over a large range of pH, demonstrated the existence of two temperature-induced domains. An inhibitor-insensitive lysozyme form was characterized at 40 degrees (physiological temperature).
D000117:Acetylglucosamine / Q000494:pharmacology; D000818:Animals; D002645:Chickens / Q000378:metabolism; D005260:Female; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009113:Muramidase / Q000378:metabolism*; D010047:Ovalbumin / Q000378:metabolism; D011487:Protein Conformation
D010047:Ovalbumin; D009113:Muramidase; D000117:Acetylglucosamine