Webber S, Hural J, Whiteley J M
Biochem Biophys Res Commun. 1987 Mar 13;143(2):582-6. doi: 10.1016/0006-291x(87)91393-3.
Cyanogen bromide cleavage of reductively alkylated homogeneous rat liver dihydropteridine reductase afforded several peptide fragments identifiable by polyacrylamide electrophoresis of which 6 (CB-1 to CB-6) could be individually isolated by C8 reverse phase HPLC. Each was characterised by N-terminal amino acid analysis and sequence information was derived for CB-1, CB-4 and CB-6. The blocked N-terminal of the holoenzyme was identified as pyroglutamate and the C-terminal sequence was obtained by sequential degradation.
用溴化氰裂解经还原烷基化的大鼠肝脏二氢蝶啶还原酶均一性产物，得到了几个可通过聚丙烯酰胺电泳鉴定的肽片段，其中6个（CB-1至CB-6）可通过C8反相高效液相色谱法单独分离。每个片段都通过N端氨基酸分析进行了表征，并获得了CB-1、CB-4和CB-6的序列信息。全酶封闭的N端被鉴定为焦谷氨酸，通过顺序降解获得了C端序列。
