The possible role of sulfhydryl groups in the adaptation of cardiac myosin to work overload has been examined. The functional integrity of sulfhydryl groups was evaluated by measurement of Ca2+- and K+-(EDTA)-ATPase activities of myosins following sulfhydryl modification. No activation of Ca2+-ATPase of normal rat cardiac myosin was observed after pMB or NEM pretreatment. The decrease in Ca2+-ATPase of myosin from hypertrophied hearts was eliminated following sulfhydryl modification: moreover, slight stimulation of Ca2+-ATPase was observed. An increase in KCl concentration did not stimulate the Ca2+-ATPase of NEM-modified myosins obtained from either control or hypertrophied hearts. The sulfhydryl content of rat cardiac myosin expressed as moles of SH per 10(5) g of myosin was 6.99 +/- 0.30 and in IPR-induced hypertrophy did not change it significantly. In the authors' opinion an alteration in the integrity of the sulfhydryl groups may be responsible for the functional partition (decreased Ca2+-ATpase with unchanged K+-[EDTA]-ATPase activity) of myosin from hypertrophied hearts.
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