Bembenek M E
Division of Medicinal Chemistry, College of Pharmacy, Univerity of Texas, Austin 78712.
Biochem Biophys Res Commun. 1990 Apr 30;168(2):702-8. doi: 10.1016/0006-291x(90)92378-d.
Adenosine plays many significant roles both as a metabolic precursor and cell communicator. This report describes the preliminary characterization of two adenosine binding proteins isolated from bovine brain membranes. By using N6-9-aminononane adenosine labeled Sepharose 4B two major affinity bound proteins were purified having apparent molecular weights of 16 and 35 kDa. Either or both of the proteins could be selectively eluted from the affinity column with N6-9-aminononane adenosine, adenosine, cAMP, AMP, ADP, ATP, R-/S-phenylisopropyladenosine and NAD(H). By contrast, no proteins were eluted with caffeine, adenine, deoxyadenosine, 2',3'-AMP, inosine, IMP, xanthine, XMP, GMP, GTP or 5'-N-ethylcarboxamideadenosine. The selectivity of elution and lack of apparent enzymatic activity suggests that these proteins are novel membrane bound adenosine binding proteins.
腺苷作为一种代谢前体和细胞通讯分子发挥着许多重要作用。本报告描述了从牛脑膜中分离出的两种腺苷结合蛋白的初步特性。通过使用N6-9-氨基壬烷腺苷标记的琼脂糖凝胶4B，纯化出了两种主要的亲和结合蛋白，其表观分子量分别为16 kDa和35 kDa。这两种蛋白中的一种或两种都可以用N6-9-氨基壬烷腺苷、腺苷、cAMP、AMP、ADP、ATP、R-/S-苯异丙基腺苷和NAD(H)从亲和柱上选择性洗脱。相比之下，咖啡因、腺嘌呤、脱氧腺苷、2',3'-AMP、肌苷、IMP、黄嘌呤、XMP、GMP、GTP或5'-N-乙基羧酰胺腺苷不能洗脱任何蛋白。洗脱的选择性和缺乏明显的酶活性表明这些蛋白是新型的膜结合腺苷结合蛋白。
