Ventura C, Bastagli L, Spampinato S, Guardigli G, Cavazza M, Bernardi P, Caldarera C M
Life Sci. 1987 Sep 7;41(10):1257-63. doi: 10.1016/0024-3205(87)90204-9.
The activity of the azide-insensitive Ca2+-dependent ATPase (highly enriched in myofibrillar ATPase activity) was studied in specimens of both right and left atria which were taken from patients with ischemic and/or valvular heart disease during coronary by pass and/or valvular substitution. A significantly lower enzymatic activity was found in atrial specimens from patients with left ventricular heart failure in comparison to the atrial fragments obtained from the patients with normal heart function. Such an inhibition reflected a significant increase in the Km of the enzyme for ATP and was associated with a concomitant reduction in Vmax, both more evident in the left atrial fragments. Moreover, tissue homogenates of atrial specimens from failing hearts exhibited a lower protein SH group content when compared to the atrial homogenates from the heart with normal left ventricular heart function.
在冠状动脉搭桥术和/或瓣膜置换术中，从患有缺血性和/或瓣膜性心脏病的患者身上获取左右心房标本，研究了叠氮化物不敏感的Ca2+依赖性ATP酶（肌原纤维ATP酶活性高度富集）的活性。与心功能正常患者的心房碎片相比，左心室心力衰竭患者的心房标本中酶活性显著降低。这种抑制反映了该酶对ATP的Km值显著增加，并伴有Vmax降低，在左心房碎片中更为明显。此外，与左心室心功能正常的心脏的心房匀浆相比，衰竭心脏的心房标本的组织匀浆中蛋白质SH基团含量较低。
