Deshpande V, Ramachandran L K
Department of Biochemistry, Osmania University, Hyderabad.
Indian J Biochem Biophys. 1990 Apr;27(2):118-20.
N-Terminal analysis of purified buffalo thyroglobulin by the fluorodinitrobenzene method of Sanger yielded about 1.5 moles of DNP-glutamic acid per mole of buffalo thyroglobulin. No water-soluble DNP-amino acid was detectable as N-terminal. The presence of glutamic acid has been confirmed by Edman degradation and characterization of the PTH-amino acid in different solvent systems, and also after regeneration of free amino acid from PTH-amino acid in butanol-acetic acid-water (4:1:5, v/v) system. This is in contrast to the occurrence of aspartic acid or asparagine as N-terminals for several other mammalian thyroglobulins.
采用桑格的氟二硝基苯法对纯化的水牛甲状腺球蛋白进行N端分析，结果显示，每摩尔水牛甲状腺球蛋白约产生1.5摩尔的DNP-谷氨酸。未检测到水溶性DNP-氨基酸作为N端。通过埃德曼降解以及在不同溶剂系统中对PTH-氨基酸的表征，并且在丁醇-乙酸-水（4:1:5，v/v）系统中从PTH-氨基酸再生游离氨基酸后，谷氨酸的存在得到了证实。这与其他几种哺乳动物甲状腺球蛋白以天冬氨酸或天冬酰胺作为N端的情况形成对比。
