Banaś T, Krotkiewska B, Marcinkowska A, Wolny M
Acta Biochim Pol. 1983;30(3-4):325-34.
Glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12) from pig muscle was inactivated by incubation with butanedione in triethanolamine buffer, pH 8.3. The inactivation was reversible after short treatment with butanedione; it became irreversible after 12-15 h, with a concomitant loss of two arginyl residues per subunit. The modified enzyme was digested with TPCK-trypsin and the peptides were purified by chromatography and electrochromatography. Two new peptides were obtained as the result of modification. From their partially determined sequence the modified arginyl residues were identified as Arg-13 and Arg-231 in the primary structure of pig muscle enzyme.
猪肌肉中的3-磷酸甘油醛脱氢酶（EC 1.2.1.12）在pH 8.3的三乙醇胺缓冲液中与丁二酮一起温育会失活。用丁二酮短暂处理后失活是可逆的；12 - 15小时后变为不可逆，每个亚基同时失去两个精氨酰残基。用TPCK - 胰蛋白酶消化修饰后的酶，通过色谱法和电色谱法纯化肽段。修饰产生了两个新的肽段。根据它们部分确定的序列，修饰后的精氨酰残基在猪肌肉酶的一级结构中被鉴定为Arg - 13和Arg - 231。
