Anderson B M, Kahn D W, Anderson C D
J Gen Microbiol. 1985 Aug;131(8):2041-5. doi: 10.1099/00221287-131-8-2041.
The 2':3'-cyclic nucleotide phosphodiesterase:3'-nucleotidase of Haemophilus influenzae was purified from a periplasmic preparation by affinity chromatographic techniques. The enzyme-catalysed hydrolysis of 2':3'-cyclic AMP to adenosine without accumulation of the intermediate substrate 3'-AMP was demonstrated by high performance liquid chromatography. Competitive inhibition of the enzyme by a variety of nucleosides and mononucleotides indicated the presence of either purine or pyrimidine bases to be essential for selective interactions with the enzyme, and confirmed the need for a 3'-position phosphate for the functioning of mononucleotides as substrates for the enzyme. The enzyme had a molecular weight of 79 000, was stable at low temperatures and was thermally denatured at temperatures above 50 degrees C.
流感嗜血杆菌的2':3'-环核苷酸磷酸二酯酶:3'-核苷酸酶通过亲和色谱技术从周质体制备物中纯化出来。高效液相色谱法证明了该酶催化2':3'-环磷酸腺苷水解为腺苷，且无中间底物3'-磷酸腺苷的积累。多种核苷和单核苷酸对该酶的竞争性抑制表明，嘌呤或嘧啶碱基的存在对于与该酶的选择性相互作用至关重要，并证实了单核苷酸作为该酶底物发挥作用需要3'-位磷酸基团。该酶的分子量为79000，在低温下稳定，在50摄氏度以上会发生热变性。
