Validation of determination of human α-amylase activity for patients with pancreatic diseas
Blood α-amylase activity is a key laboratory marker of pancreatic diseases. At the same time, some of the common laboratory methods of its measurement have a number of limitations. Therefore new more effective laboratory methods are currently being developed over those methods that have been already...
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| Format: | Article |
| Language: | Russian |
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Russian Academy of Sciences, Siberian Branch Publishing House
2021-08-01
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| Series: | Сибирский научный медицинский журнал |
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| Online Access: | https://sibmed.elpub.ru/jour/article/view/640 |
| _version_ | 1797269548138758144 |
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| author | K. A. Cheremisina E. G. Yakovleva A. V. Baraboshkina E. F. Agletdinov |
| author_facet | K. A. Cheremisina E. G. Yakovleva A. V. Baraboshkina E. F. Agletdinov |
| author_sort | K. A. Cheremisina |
| collection | DOAJ |
| description | Blood α-amylase activity is a key laboratory marker of pancreatic diseases. At the same time, some of the common laboratory methods of its measurement have a number of limitations. Therefore new more effective laboratory methods are currently being developed over those methods that have been already available. The aim of this work was to compare two methods of determination of the activity of total and pancreatic α-amylase in human blood based on using 4,6-ethylidene-(G7)-p-nitrophenyl-(G1)-α,D-maltoheptaoside (EPS-G7) and 2-chloro-4-nitrophenyl-4-O-β-D-galactopyranosylmaltoside (GalG2CNP) as substrates. Blood serum samples from patients with different levels of α-amylase activity were analyzed. The main analytical characteristics of the method with the GalG2CNP substrate were determined using purified α-amylase specimens. A high-sized correlation and high accuracy of the α-amylase isoenzymes activity were observed for the both methods. Therefore, the method for determining the activity of α-amylase using GalG2CNP as a substrate has analytical characteristics similar to the common laboratory method with EPS-G7, but at the same time, the existing advantages allow it to be recommended for wider application in clinical laboratory diagnostics and scientific research. |
| first_indexed | 2024-03-08T14:34:16Z |
| format | Article |
| id | doaj.art-aef15daf652549528b576db695b09260 |
| institution | Directory Open Access Journal |
| issn | 2410-2512 2410-2520 |
| language | Russian |
| last_indexed | 2024-04-25T01:50:07Z |
| publishDate | 2021-08-01 |
| publisher | Russian Academy of Sciences, Siberian Branch Publishing House |
| record_format | Article |
| series | Сибирский научный медицинский журнал |
| spelling | doaj.art-aef15daf652549528b576db695b092602024-03-07T18:49:59ZrusRussian Academy of Sciences, Siberian Branch Publishing HouseСибирский научный медицинский журнал2410-25122410-25202021-08-01414798510.18699/SSMJ20210411371Validation of determination of human α-amylase activity for patients with pancreatic diseasK. A. Cheremisina0E. G. Yakovleva1A. V. Baraboshkina2E. F. Agletdinov3JSC Vector-BestJSC Vector-BestJSC Vector-BestJSC Vector-BestBlood α-amylase activity is a key laboratory marker of pancreatic diseases. At the same time, some of the common laboratory methods of its measurement have a number of limitations. Therefore new more effective laboratory methods are currently being developed over those methods that have been already available. The aim of this work was to compare two methods of determination of the activity of total and pancreatic α-amylase in human blood based on using 4,6-ethylidene-(G7)-p-nitrophenyl-(G1)-α,D-maltoheptaoside (EPS-G7) and 2-chloro-4-nitrophenyl-4-O-β-D-galactopyranosylmaltoside (GalG2CNP) as substrates. Blood serum samples from patients with different levels of α-amylase activity were analyzed. The main analytical characteristics of the method with the GalG2CNP substrate were determined using purified α-amylase specimens. A high-sized correlation and high accuracy of the α-amylase isoenzymes activity were observed for the both methods. Therefore, the method for determining the activity of α-amylase using GalG2CNP as a substrate has analytical characteristics similar to the common laboratory method with EPS-G7, but at the same time, the existing advantages allow it to be recommended for wider application in clinical laboratory diagnostics and scientific research.https://sibmed.elpub.ru/jour/article/view/640pancreatitislaboratory diagnosticsα-amylaseactivityisoenzymesubstrate |
| spellingShingle | K. A. Cheremisina E. G. Yakovleva A. V. Baraboshkina E. F. Agletdinov Validation of determination of human α-amylase activity for patients with pancreatic diseas Сибирский научный медицинский журнал pancreatitis laboratory diagnostics α-amylase activity isoenzyme substrate |
| title | Validation of determination of human α-amylase activity for patients with pancreatic diseas |
| title_full | Validation of determination of human α-amylase activity for patients with pancreatic diseas |
| title_fullStr | Validation of determination of human α-amylase activity for patients with pancreatic diseas |
| title_full_unstemmed | Validation of determination of human α-amylase activity for patients with pancreatic diseas |
| title_short | Validation of determination of human α-amylase activity for patients with pancreatic diseas |
| title_sort | validation of determination of human α amylase activity for patients with pancreatic diseas |
| topic | pancreatitis laboratory diagnostics α-amylase activity isoenzyme substrate |
| url | https://sibmed.elpub.ru/jour/article/view/640 |
| work_keys_str_mv | AT kacheremisina validationofdeterminationofhumanaamylaseactivityforpatientswithpancreaticdiseas AT egyakovleva validationofdeterminationofhumanaamylaseactivityforpatientswithpancreaticdiseas AT avbaraboshkina validationofdeterminationofhumanaamylaseactivityforpatientswithpancreaticdiseas AT efagletdinov validationofdeterminationofhumanaamylaseactivityforpatientswithpancreaticdiseas |