Nicholson J A, Peters T J
Clin Chim Acta. 1979 Jan 15;91(2):153-8. doi: 10.1016/0009-8981(79)90450-9.
A sensitive but simple fluorimetric assay for intestinal enzymes capable of hydrolysing certain glycine-containing peptides is described. In the standard assay, 1 nanomole of glycine can be accurately estimated in the presence of a 2000-fold molar excess of unhydrolysed peptide. Initial rates of peptide hydrolysis can be measured on the density gradient fractions obtained by analytical subcellular fractionation of extracts from milligram quantities of human jejunal tissue. Differences in the subcellular localisation of activity against two peptides are illustrated. The implications of these findings in relation to the study of intestinal peptidase deficiency in disease states are discussed.
本文描述了一种灵敏且简单的荧光测定法,用于检测能够水解某些含甘氨酸肽的肠道酶。在标准测定中,在存在2000倍摩尔过量未水解肽的情况下,可准确估算1纳摩尔甘氨酸。肽水解的初始速率可在通过对毫克量人空肠组织提取物进行分析性亚细胞分级分离得到的密度梯度级分上进行测量。说明了针对两种肽的活性在亚细胞定位上的差异。讨论了这些发现与疾病状态下肠道肽酶缺乏研究的相关性。