Shephard M D, Peake M J
J Clin Pathol. 1986 Sep;39(9):1025-30. doi: 10.1136/jcp.39.9.1025.
The potential use of the protein denaturant guanidine hydrochloride to inhibit selectively the enzyme activity of serum alkaline phosphatase isoenzymes from liver, bone, intestine, and placenta was investigated. Inhibition of each isoenzyme was shown to be dependent on time and concentration of inhibitor. In the presence of 0.3 mol/l (28.7 g/l) guanidine hydrochloride for 170 seconds 14%, 47%, and 90% of the total alkaline phosphatase activity remained in samples of bone, liver, and intestinal origins, respectively. In contrast, the activity of the placental isoenzyme increased by 24%. The degree of inhibition was shown to be independent of total alkaline phosphatase activity. Investigations were performed at 37 degrees C using the Cobas Bio centrifugal analyser. We conclude that this reagent has several practical advantages over urea as a selective inhibitor of alkaline phosphatase isoenzymes, including a faster and more reproducible inhibition at a much lower reagent concentration.
研究了蛋白质变性剂盐酸胍选择性抑制来自肝脏、骨骼、肠道和胎盘的血清碱性磷酸酶同工酶活性的潜在用途。结果表明，每种同工酶的抑制作用取决于抑制剂的时间和浓度。在存在0.3mol/L（28.7g/L）盐酸胍的情况下作用170秒后，骨、肝脏和肠道来源的样品中分别保留了14%、47%和90%的总碱性磷酸酶活性。相比之下，胎盘同工酶的活性增加了24%。抑制程度与总碱性磷酸酶活性无关。使用Cobas Bio离心分析仪在37℃下进行研究。我们得出结论，作为碱性磷酸酶同工酶的选择性抑制剂，该试剂比尿素具有几个实际优势，包括在低得多的试剂浓度下抑制作用更快且更可重复。
