Gutowicz J, Modrzycka T
Biochim Biophys Acta. 1978 Sep 11;512(1):105-10. doi: 10.1016/0005-2736(78)90221-3.
The binding of glyceraldehyde-3-phosphate dehydrogenase prepared from rabbit muscle to phospholipid model membranes (liposomes) as a function of pH, ionic strength, and the influence of the binding on specific activity of the enzyme was studied. The binding decreases the specific activity of the enzyme. The binding was studied by the method of association of the enzyme with liposomes during centrifugation. The existence of a dominant interaction of electrostatic character was found.
研究了从兔肌肉中制备的甘油醛-3-磷酸脱氢酶与磷脂模型膜(脂质体)的结合情况,该结合是pH值、离子强度的函数,并研究了这种结合对酶比活性的影响。这种结合降低了酶的比活性。通过在离心过程中使酶与脂质体缔合的方法来研究这种结合。发现存在一种主要的静电相互作用。