Development and application of a histidine-selective biomembrane electrode.
Development and application of a histidine-selective biomembrane electrode.
复制标题
DOI：
10.1021/ac00239a016
复制
发表时间：
1982-02
影响因子：
7.4
通讯作者：
P. Kovach;M. Meyerhoff
中科院分区：
文献类型：
--
作者：
P. Kovach;M. Meyerhoff
A highly selective histidine biomembrane electrode has been prepared by Immobilizing the enzyme histidine decarboxylase (EC No. 4.1. 1.22) at the surface of a potentiometric carbon dioxide sensor. The enzyme employed was extracted from Lactobacillus 30a. The use of concentrated enzymeextract rather than Intact bacterial cells Is shown to yield bloelectrodes with Improved response characteristics. The resulting enzyme-based sensor responds linearly to the logarithm of¿.-histidine concentration between 3 X 10~ 4 and 1 X 10~ 2 mol/L with a slope typically of 48-53 mV/decade and a useful lifetime of over 30days. The electrode can be used to assay histidine directly In urine samples with good analytical re-covery (av 104.8%) and correlation (r= 0.91) with a fluorometric procedure.The development of enzyme-, bacterial-, and tissue-based biomembrane electrodes selective for physiologically important compounds continues to be an expanding and exciting area of research (1-5). To be of practical analytical utility, such electrodes must possess certain desirable response charac-teristics including high selectivity, rapid response times, freedom from inhibitor interferences which may be present in real samples, andlong-term stability. We now report the development of a new histidine-selective biomembrane elec-trode which appears to meet these requirements (histidine refers to the physiologically active form, L-histidine). Several workers have previously reported histidine-selective electrodes based on immobilized enzyme or bacterial cell catalyzed reactions (6-8). Buck et al. utilized histidine am-monialyase (EC No. 4.3. 1.3) from Pseudomonas sp. to de-velop a histidine electrode which relied on a potentiometric ammonia gas sensoras the detector (6). The intact cells were also employed for the construction of the electrode, but se-lectivity was poor because of the presence of other deaminating enzymes (7). White (8), used histidine decarboxylase purified from Ch. Welchii in conjunction with a potentiometric carbon dioxide sensor to prepare a histidine electrode. The electrode had reasonable response times (approximately 10 min), a good dynamic response range, andselectivity over other common amino acids. However, no information concerning response to histidine derivatives or similar compounds was provided. In addition, in that work, and in other histidine electrode reports, no real sample analytical utility was demonstrated. Histidine measurements in serum and urine samples are associated with the diagnosis of histidine metabolism disor-ders, particularly histidemia (9, 10). Elevated levels in physiological fluids signal this hereditary disease. Current ion exchange chromatography (11) or fluorometric reaction procedures (12, 13) used to determine histidine in clinical samples are complex and time-consuming and, in the case of fluorescence, require causticanalytical reagents. In this paper, the development, study and analytical ap-
