Campos M, Alarcón M, González H
Department of Chemistry, Faculty of Sciences, University of Concepción, Casilla, Chile.
Microbios. 1990;63(254):29-35.
The beta-lactamase from Shigella flexneri UCSF-129 was irreversible inactivated by 6-beta-iodopenicillanic acid. Only one serine residue was modified, according to the spectra change and the amino acid analyses. A pH variation of 0.3 units was found when the chemically modified enzyme was submitted to isoelectric focusing. The inactivation constant of the fast time course reaction was 0.1 seg-1. Protection of 96% was obtained, using cephradine 2,830 times more concentrated than 6-beta-iodopenicillanic acid. It is suggested that this enzyme belongs to class A, according to Ambler (1980).
弗氏志贺菌UCSF - 129的β-内酰胺酶被6-β-碘青霉烷酸不可逆地灭活。根据光谱变化和氨基酸分析,只有一个丝氨酸残基被修饰。当化学修饰的酶进行等电聚焦时,发现pH值有0.3个单位的变化。快速时程反应的失活常数为0.1秒⁻¹。使用浓度比6-β-碘青霉烷酸高2830倍的头孢拉定可获得96%的保护率。根据安布勒(1980年)的分类,推测该酶属于A类。