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Abstract
Trypsin fragments carp myosin heavy chain into components of lower molecular weight. These changes are concomitant with the loss of Ca2+-ATPase and a weakening in actin-myosin interaction. As heavy meromyosin (HMM) prepared from myofibrils is more homogeneous, the above changes are due to overfragmentation of heavy chain mass. Amino-acid composition of carp and rabbit HMM's are similar, but differences exist in response to DTNB and incorporation.