Sakai T, Yanagihara S, Kunugi Y, Ushio K
Br J Ind Med. 1982 Nov;39(4):382-7. doi: 10.1136/oem.39.4.382.
Proteins in the ALA-D (delta-aminolaevulinic acid dehydratase) fraction from gel filtration of erythrocyte supernatant (ES) have the highest affinity for lead among erythrocyte constituents in vivo and in vitro. It takes 20-40 hours for erythrocyte components to be equilibrated with lead added in vitro. AT low lead concentrations, under 60 micrograms/100 ml ES, the extent of decrease in ALA-D activity indicates the extent of lead saturation of ALA-D fraction proteins. The saturation is attained at 80-110 micrograms/100 ml ES. Although an appreciable amount of lead is also found in the haemoglobin fraction that contains certain factors concerned in ALA-D inhibition, lead responsible for inducing the inhibition is not bound to haemoglobin fraction proteins but to ALA-D fraction proteins. Of three treatments or agents recovering the enzyme from lead effects, zinc is the only one that can fully restore the inhibition.
红细胞上清液(ES)经凝胶过滤后,δ-氨基乙酰丙酸脱水酶(ALA-D)组分中的蛋白质在体内和体外的红细胞成分中对铅具有最高的亲和力。红细胞成分与体外添加的铅达到平衡需要20 - 40小时。在低铅浓度下,即低于60微克/100毫升ES时,ALA-D活性的降低程度表明ALA-D组分蛋白质的铅饱和程度。在80 - 110微克/100毫升ES时达到饱和。虽然在含有某些与ALA-D抑制有关因素的血红蛋白组分中也发现了相当数量的铅,但导致抑制的铅并非与血红蛋白组分蛋白质结合,而是与ALA-D组分蛋白质结合。在三种使酶从铅的影响中恢复的处理方法或试剂中,锌是唯一能完全恢复抑制作用的一种。