Khan A A, Schuler M M, Coppock R W
Animal Sciences Wing, Alberta Environmental Centre, Vegreville, Alberta, Canada.
J Toxicol Environ Health. 1987;22(4):481-90. doi: 10.1080/15287398709531087.
Studies were conducted to assess the in vitro effects of selected sulfur compounds on the activities of superoxide dismutase (SOD), catalase, glutathione peroxidase (GSHPX), and glucose-6-phosphate dehydrogenase (G6PDH) in hemolyzates of bovine erythrocytes. All sulfur compounds produced concentration-dependent inhibition in the activities of these enzymes, but their effects on each enzyme were different. SOD and catalase activities were most sensitive to sulfide (S2-), followed by sulfite (SO3(2-)) and sulfate (SO4(2-)). GSHPX activity was most sensitive to SO3(2-), followed by S2-, cysteine and SO4(2-). The activity of G6PDH, however, was maximally inhibited by reduced glutathione (GSH), followed by SO3(2-) and SO4(2-); S2- was inhibitory only at high concentrations. Dialysis of the S2- and SO3(2-)-inhibited enzymes resulted in complete or partial reversal of inhibitory effects. The biochemical significance of these effects in relation to erythrocyte physiology is discussed.
开展了多项研究，以评估特定含硫化合物对牛红细胞溶血产物中超氧化物歧化酶（SOD）、过氧化氢酶、谷胱甘肽过氧化物酶（GSHPX）和葡萄糖-6-磷酸脱氢酶（G6PDH）活性的体外影响。所有含硫化合物均对这些酶的活性产生浓度依赖性抑制作用，但它们对每种酶的影响各不相同。SOD和过氧化氢酶的活性对硫化物（S2-）最为敏感，其次是亚硫酸盐（SO3(2-)）和硫酸盐（SO4(2-)）。GSHPX的活性对SO3(2-)最为敏感，其次是S2-、半胱氨酸和SO4(2-)。然而，G6PDH的活性受到还原型谷胱甘肽（GSH）的最大抑制，其次是SO3(2-)和SO4(2-)；S2-仅在高浓度时具有抑制作用。对受S2-和SO3(2-)抑制的酶进行透析，可使抑制作用完全或部分逆转。本文讨论了这些作用与红细胞生理学相关的生化意义。
