Long S D, Rodrick G E, Friedl F E
Comp Biochem Physiol B. 1984;78(2):467-72. doi: 10.1016/0305-0491(84)90060-9.
The specific activities, kinetic constants and pH optima for succinate dehydrogenase were determined in mantle, gill and adductor muscle from three bivalves (Anodonta couperiana, Elliptio buckleyi and Mercenaria campechiensis). In general the Km values for succinate and Ki values for fumarate differed in all bivalve tissues whereas the Ki for malonate was consistently low. The ratio of Ki (fumarate) to Km (succinate) was less than one for all tissues studied. This is similar to many facultative anaerobes with fumarate reductase activity.
测定了三种双壳贝类(库氏无齿蚌、巴氏椭圆蚌和坎佩切湾硬壳蛤)外套膜、鳃和闭壳肌中琥珀酸脱氢酶的比活性、动力学常数和最适pH值。总体而言,所有双壳贝类组织中琥珀酸的Km值和富马酸的Ki值有所不同,而丙二酸的Ki值一直较低。在所研究的所有组织中,富马酸的Ki与琥珀酸的Km之比均小于1。这与许多具有富马酸还原酶活性的兼性厌氧菌相似。