β-galactosidase activated by sodium ions can catalyze o-nitrophenol to produce glycoside and o-nitrophenol. The increase of absorbance is determined at 405 nm, and the content of sodium ion is calculated indirectly.
The formation of nitrophenol from the substrate nitropyranoside is catalyzed by sodium-activated β-galactosidase. The increase rate of absorbance value of nitrophenol at 405 nm per unit time was proportional to the sodium concentration.
Soluble Starch Synthase (SSS) catalyzes the reaction between ADPG and the primer, transfers glucose molecules to the primer, and simultaneously generates ADP, which in turn catalyzes the reduction of NADP+ to NADPH. The amount of NADPH produced is proportional to the amount of ADP produced in the previous reaction. SSS activity was calculated by measuring the increase in NADPH at 340 nm.
Sphingomyelin (SM) is widely present in cell membranes and plasma lipoproteins. Metabolism of SM is regulated by sphingomyelin synthase and sphingomyelase, whose metabolites include ceramide, sphingosinol and choline phosphate, which are important second messengers. Studies have shown that SM and its metabolites play an important role in liver, lung, and cardiovascular diseases. The principle of this kit is that SM is catalyzed by sphingomyelin enzyme, and its products generate fluorescent substances with the probe under the action of other enzymes. By substituting the fluorescence value into the standard curve, SM content in the sample can be calculated.
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