Tsuchiya M, Osago H, Shimoyama M
Department of Biochemistry, Shimane Medical University, Izumo, Japan.
Biochem Biophys Res Commun. 1995 Sep 25;214(3):760-4. doi: 10.1006/bbrc.1995.2351.
Arginine-specific ADP-ribosyltransferase activity was detected in chicken spleen membrane fraction and the activity was extracted by phosphatidylinositol-specific phospholipase C but not by 1 M NaCl or 1% Triton X-100. The transferase activity extracted from the spleen membrane was thiol-independent and was not inhibited by 200 mM NaCl. Zymographic analysis of the transferase, under non-reducing conditions, showed two forms of active bands corresponding to a molecular mass of 46 and 42 kDa. Thus, the presence of this novel arginine-specific ADP-ribosyltransferase, anchored to the membrane through glycosylphosphatidylinositol and different from previously cloned chicken transferases, AT1 and AT2, is being given further attention.
在鸡脾脏膜组分中检测到精氨酸特异性ADP核糖基转移酶活性,该活性可被磷脂酰肌醇特异性磷脂酶C提取,但不能被1M NaCl或1% Triton X-100提取。从脾脏膜中提取的转移酶活性不依赖巯基,且不受200mM NaCl抑制。在非还原条件下对转移酶进行酶谱分析,显示出两种活性条带形式,对应分子量分别为46 kDa和42 kDa。因此,这种通过糖基磷脂酰肌醇锚定在膜上、不同于先前克隆的鸡转移酶AT1和AT2的新型精氨酸特异性ADP核糖基转移酶的存在正受到进一步关注。