Schaefer J, Garbow J R, Jacob G S, Forrest T M, Wilson G E
Biochem Biophys Res Commun. 1986 Jun 13;137(2):736-41. doi: 10.1016/0006-291x(86)91140-x.
Lyophilized whole cells of Aerococcus viridans (Gaffkya homari) grown on a synthetic medium containing D-[2-13C, 15N]Ala, or containing both L-[1-13C]Lys and D-[15N]Ala, have been examined by double cross-polarization magic-angle spinning 13C and 15N nuclear magnetic resonance. Results from the double-labeled alanine experiment confirm the absence of metabolic scrambling of alanine by A. viridans. Results from the combined single-label experiment can be used to count directly the number of adjacent L-Lys and D-Ala units in peptide chains of cell-wall peptidoglycan. This count leads to the conclusion that there are no terminal D-Ala or D-Ala-D-Ala units in uncross-linked chains of the peptidoglycan of A. viridans.
已通过双交叉极化魔角旋转13C和15N核磁共振对在含有D-[2-13C, 15N]丙氨酸或同时含有L-[1-13C]赖氨酸和D-[15N]丙氨酸的合成培养基上生长的绿色气球菌（龙虾气球菌）冻干全细胞进行了检测。双标记丙氨酸实验的结果证实了绿色气球菌不存在丙氨酸的代谢混编。联合单标记实验的结果可用于直接计算细胞壁肽聚糖肽链中相邻L-赖氨酸和D-丙氨酸单元的数量。这一计算得出的结论是，绿色气球菌肽聚糖未交联链中不存在末端D-丙氨酸或D-丙氨酸-D-丙氨酸单元。
