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基于 B 掺杂核壳结构 Fe@BC 纳米酶的比色法测定丙氨酸氨基转移酶。

Optical assay using B-doped core-shell Fe@BC nanozyme for determination of alanine aminotransferase.

机构信息

Key Laboratory of Transplantation, Chinese Academy of Medical Sciences, Beijing, 100730, China.

Tianjin Key Laboratory for Organ Transplantation, Department of Liver Transplantation, Tianjin First Center Hospital, Tianjin, 300192, China.

出版信息

Mikrochim Acta. 2022 Mar 17;189(4):147. doi: 10.1007/s00604-021-05056-w.

DOI:10.1007/s00604-021-05056-w
PMID:35299258
Abstract

B-doped core-shell Fe@BC nanozyme was synthesized. The peroxidase (POD) like activity of Fe@BC nanozyme was studied and utilized for detecting the activity of alanine aminotransferase (ALT). In the presence of ALT as well as ALT co-substrates L-alanine and α-ketoglutarate, L-glutamate is generated. The following catalytic oxidation of L-glutamate by glutamate oxidase leads to the generation of HO. The POD-like activity of Fe@BC can oxidize 3,3',5,5'-tetramethylbenzidine (TMB) to oxTMB in the presence of HO, generating a blue-colored compound. Through the detection of the amount of HO generated, ALT activity can be determined through measuring the absorbance intensity variation at 450 nm. The limit of detection of the assay is 4 U/L, with a linear range from 10 to 1000 U/L. For human serum samples, the ALT levels determined by our assay are comparable to those determined by the hospital with a correlation coefficient of 0.991, demonstrating the reliability of our assay results.

摘要

B 掺杂核壳结构 Fe@BC 纳米酶的合成。研究了 Fe@BC 纳米酶的过氧化物酶(POD)样活性,并将其用于检测丙氨酸氨基转移酶(ALT)的活性。在 ALT 以及 ALT 共底物 L-丙氨酸和α-酮戊二酸存在的情况下,生成 L-谷氨酸。随后,L-谷氨酸被谷氨酸氧化酶催化氧化生成 HO。在 HO 的存在下,Fe@BC 的 POD 样活性可以将 3,3',5,5'-四甲基联苯胺(TMB)氧化为 oxTMB,生成蓝色化合物。通过检测生成的 HO 的量,可以通过测量 450nm 处吸光度强度的变化来确定 ALT 活性。该测定方法的检测限为 4U/L,线性范围为 10 至 1000U/L。对于人血清样本,我们的测定方法所确定的 ALT 水平与医院的测定结果相当,相关系数为 0.991,表明我们的测定结果可靠。

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