Early structural changes in myosin rod upon heating of carp myofibrils.
Upon heating carp myofibrils at 40 degrees C, the amount of myosin that is soluble and monomeric dropped very quickly, roughly 5 times faster than the ATPase inactivation. This rapid decrease of solubility was well explained by a rapid denaturation of the rod portion as measured by chymotryptic digestibility. Chymotryptic digestion of heated myofibrils in a low-salt medium with EDTA generated a reduced amount of rod and subfragment-1 (S-1). The decrease of S-1 produced from the heated myofibrils was consistent with the ATPase inactivation. The decrease of rod produced from the heated myofibrils was explained by the increased susceptibility of the heavy meromyosin (HMM)/light meromyosin (LMM) junction to chymotryptic. It was, therefore, concluded that the fastest event occurring in the myosin molecule upon heating of myofibrils is the irreversible exposure of the HMM/LMM junction.
Konno
K
K
Laboratory of Food Biochemistry, Faculty of Fisheries, Hokkaido University, Hakodate, Hokkaido 041-8611 Japan. konno@fish.hokudai.ac.jp
Yamamoto
T
T
Takahashi
M
M
Kato
S
S
D000818:Animals; D002347:Carps / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D009210:Myofibrils / Q000737:chemistry*; D009218:Myosins / Q000737:chemistry*; D011487:Protein Conformation; D011489:Protein Denaturation
D009218:Myosins