The reducing sugar reacts with 3,5-dinitrosalicylic acid under heating conditions to produce a brown-red substance, which is inactivated by the thermolabile nature of β-amylase, and then the enzyme activity of α-amylase is determined.
The reducing sugar reacts with 3,5-dinitrosalicylic acid under heating conditions to produce a brown-red substance. Amylase activity can be calculated by measuring the OD value at 540 nm.
α-Galactosidase (α-Gal) catalyzes the substances produced in the glycolysis process of animal and plant tissues to form the final product, which has a maximum absorption peak at 405 nm.
α-Glucosidase (α-GC), also known as α-D-glucoside hydrolase, is widely distributed in nature, with a wide variety of species and different properties, and exists in almost all organisms. It has important physiological functions in carbohydrate metabolism in animals, plants and microorganisms. If α-GC is deficient, it leads to severe glycogen metabolism disorders and excessive glycogen accumulation, which can cause Pompah's disease (an autosomal recessive inherited glycogen storage disease, also known as glycogenosis type II). Long-term low α-GC activity in human tissues can cause muscle fiber destruction and muscle atrophy. The detection principle of this kit is that the chromogenic substance generated by the substrate reaction catalyzed by α-glucosidase has the maximum absorption at 400 nm, and the enzyme activity of α-GC can be reflected by measuring its OD value at 400 nm.
α-Hydroxybutyrate Dehydrogenase (α-HBDH) is a general term for Lactic Dehydrogenase (LDH) isoenzymes LDH 1 and LDH 2, and is one of the five components of the myocardial enzyme spectrum. The increase of serum creatinine is common in myocardial infarction, liver parenchymal cell lesions, rheumatic myocarditis, viral myocarditis, hemolytic anemia and other diseases. α-HBDH catalyzes the reduction of α-ketobutyric acid to α-hydroxybutyric acid in the presence of reduced coenzyme Ⅰ (NADH), and NADH is oxidized to NAD+ at a rate proportional to the enzyme activity. The activity of α-HBDH can be calculated by monitoring the rate of NADH reduction at 340 nm.
α-ketoglutarate dehydrogenase (α-KGDH) is a key enzyme in the tricarboxylic acid (TCA) cycle. While the substrate being catalyzed by α-KGDH, NAD+ is reduced to NADH, and electrons are transfered to WST-8 under the action of hydrogen transmitter to produce yellow product. The activity of α-KGDH can be calculated by measuring the change of absorbance value at 450 nm
α-Ketoglutaric acid and alanine can be combined with fluorescent probe products under the action of a series of enzymes. The content of α-ketoglutaric acid in samples can be determined by measuring the fluorescence value.
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