McIntire W, Singer T P, Ameyama M, Adachi O, Matsushita K, Shinagawa E
Biochem J. 1985 Nov 1;231(3):651-4. doi: 10.1042/bj2310651.
An improved method is presented for the purification of 8 alpha-(N1-histidyl)riboflavin, 8 alpha-(N3-histidyl)riboflavin and their 2',5'-anhydro forms, which permits the isolation of sizeable quantities of each of these compounds from a synthetic mixture in pure form. Flavin peptides were isolated from the D-gluconate dehydrogenases of Pseudomonas aeruginosa and Pseudomonas fluorescens and from the 2-keto-D-gluconate dehydrogenase of Gluconobacter melanogenus. After conversion into the aminoacyl-riboflavin, the flavin in all three enzymes was identified as 8 alpha-(N3-histidyl)riboflavin. By sequential treatment with nucleotide pyrophosphatase and alkaline phosphatase, the flavin in each enzyme was shown to be in the dinucleotide form.
本文提出了一种改进的方法用于纯化8α-(N1-组氨酰)核黄素、8α-(N3-组氨酰)核黄素及其2',5'-脱水形式，该方法能够从合成混合物中以纯形式分离出相当数量的上述每种化合物。从铜绿假单胞菌和荧光假单胞菌的D-葡萄糖酸脱氢酶以及产黑色素葡萄糖杆菌的2-酮-D-葡萄糖酸脱氢酶中分离出黄素肽。在转化为氨酰核黄素后，这三种酶中的黄素均被鉴定为8α-(N3-组氨酰)核黄素。通过依次用核苷酸焦磷酸酶和碱性磷酸酶处理，表明每种酶中的黄素均为二核苷酸形式。
