STUDY OF ATP EFFECTS ON CONFORMATION STABILITY OF THE SARCOPLASMIC RETICULUM MEMBRANE PROTEIN
ATP稳定肌浆网膜蛋白色氨酸相关构象的机理的探讨

Stearylamine and oleylamine. C18 saturated and cis -monounsaturated amines, with positive charges. were found to decline the intensity of the intrinsic protein fluorescence of skeletal muscle sarcoplasmic reticulum (SR) in the absence of ATP. When ATP or anion compounds, such as phosphate and oxalate. were added into reaction solution prior to the addition of these amines. the descended extents of fluorescence intensity induced by Stearylamine or oleylamine were decreased. which is called antagonism in this study, and the antagonism to stearylamine was stronger than that to oleylamine. Adenosine had no effect on the falls of fluorescence intensity caused by both the amines. After incubation of SR with Stearylamine. addition of ATP or anion compounds did not antagonize the fall of fluorescence intensity induced by Stearylamine. Inconsistent with Stearylamine. after incubation of SR with oleylamine, the fall of fluorescence intensity induced by oleylamine was antagonized by ATP.but not by anion compounds. The incubation of SR with ADP and GTP.which have their corresponding binding sites on SR Ca2+,Mg2+ -ATPase. respectively. antagonized the fall of fluorescence intensity induced by oleylamine significantly. While in case of .AMP. the antagonism was not observed. These results suggested that ATP may stabilize the membrane protein conformation in sarcoplasmic reticulum and the antagonism of ATP to Stearylamine may mainly depend on the negative charges in the molecule, whereas that to oleylamine may be due to substrate protection through the conformational change of calcium pump protein.