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研究了溶菌酶 ( Lysozyme,LE)在 KIO3存在下的极谱催化波 .在 0 .1 mol/ L HAc-Na Ac( p H4 .7±0 .1 )缓冲液中 ,LE有 1个由 Cys6～ Cys1 2 7间双硫键还原产生的可逆波 .其峰电位为 -0 .51 V( vs.Ag/Ag Cl) .当 KIO3存在时 ,在原电位处产生了 LE的极谱催化波 .该催化波是由于 KIO3及其中间价态衍生质点 (包括自由基 IO-· ,IO-·2 )氧化 LE还原产物巯基成双硫键所致 .这是蛋白质极谱催化波的一种新类型 .在 0 .1 mol/ L HAc-Na Ac( p H 4 .7± 0 .1 ) -1× 1 0 - 3mol/ L KIO3支持电解质中 ,LE催化波的灵敏度比其还原波的高两个数量级 ,峰电流与 LE浓度在 2× 1 0 - 7～ 1 .0× 1 0 - 6 mol/ L范围内有线性关系 .1 0 0倍半胱氨酸和胱氨酸不干扰 1 .0× 1 0 - 6 mol/ L LE的测定
The polarographic catalytic wave of Lysozyme (LE) in the presence of KIO3 was studied. In 0.1 mol / L HAc-Na Ac (p H4 .7 ± 0.1) buffer, The reversible wave produced by the reduction of the disulfide bond between Cys1 and Cys1 has a peak potential of -0.51 V (vs. Ag / Ag Cl). When KIO3 is present, a polarographic catalytic wave of LE is produced at the primary potential The catalytic wave is due to KIO3 and its intermediate valence state derived particles (including free radicals IO- ·, IO- · 2) oxidation of LE reduction product of the sulfhydryl double disulfide bond, which is a new type of polarographic catalytic wave protein. In 0.1 mol / L HAc-Na Ac (p H 4 .7 ± 0 .1) -1 × 10 3 mol / L KIO 3 support electrolyte, the sensitivity of LE catalysis wave is two orders of magnitude higher than that of the reduction wave , And the peak current was linear with the concentration of LE in the range of 2 × 10 7 ~ 1 × 10 6 mol / L. 1 0 0 cysteine and cystine did not interfere with 1.0 × 1 Determination of 0 - 6 mol / L LE