Lehmann J, Schiltz E, Steck J
Institut für Organische Chemie und Biochemie der Universität Freiburg, Germany.
Carbohydr Res. 1992 Jul 20;232(1):77-87. doi: 10.1016/s0008-6215(00)90995-9.
Four malto-oligosaccharides (dp 2-5), each with a 4,6-O-ethylidene group on the glucosyl unit at the non-reducing terminus, were synthesised and used to prove that the maltose-binding protein (MBP) of E. coli is a closed-groove binder. alpha-D-Glucosylation of 3-azibutyl 1-thio-alpha-D-(6-3H)glucopyranoside yielded a 3H-labelled, photolabile 1-thiomaltoside derivative that was used to chemically modify the binding site of MBP. The 3H-labelled peptide containing 83% of the total radioactivity, which was isolated after tryptic cleavage of the modified MBP and sequenced, is part of the closed end of the MBP groove.
合成了四种麦芽寡糖（聚合度2 - 5），每种在非还原末端的葡萄糖基单元上都带有一个4,6 - O - 亚乙基基团，并用于证明大肠杆菌的麦芽糖结合蛋白（MBP）是一种封闭凹槽结合蛋白。3 - 叠氮丁基1 - 硫代 - α - D -（6 - 3H）吡喃葡萄糖苷的α - D - 葡萄糖基化产生了一种3H标记的、光不稳定的1 - 硫代麦芽糖苷衍生物，该衍生物用于化学修饰MBP的结合位点。经胰蛋白酶切割修饰后的MBP并测序后分离得到的含有总放射性83%的3H标记肽段，是MBP凹槽封闭端的一部分。
