Abstract
Myofibrillar proteins from ox muscle are found to be most soluble in M -potassium chloride at pH 6.0. At low ionic strength the myofibrils disperse at pH values below 4.4 and above 10.1. Sarcoplasmic proteins are denatured readily at pH values below 6.0 at 37[degree] and at higher temperatures more independently of pH. Denaturation of sarcoplasmic protein in situ is associated with decreased myofibrillar solubility in M-potassium chloride. Starch-gel electrophoresis indicates one major and several minor proteins that are specifically denatured in conditions of low pH and high temperature; the major one has been identified as ATP-creatine phosphotransferase.