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Enzyme Activity Measurement for Alpha-N-Acetylgalactosaminidase

Creative Enzymes has been active in the enzyme industry and focusing on enzyme activity measurement for many years. Extensive and professional experiences help us gain a good reputation in the global market. We are specialized in developing innovative assay methods to satisfy challenging service request. We are proud to offer the most reliable enzyme activity measurement for hydrolysas such as alpha-N-acetylgalactosaminidase.

Alpha-N-acetylgalactosaminidase (EC 3.2.1.49; alpha-N-acetyl-D-galactosaminide N-acetylgalactosaminohydrolase), which cleaves α-linked N-acetylgalactosaminyl units from glycoproteins and glycolipids, is widely distributed among living organisms and is involved in the metabolism of glycoconjugates. Alpha-N-acetylgalactosaminidase has been identified and purified from a variety of species including bacteria, protozoa, gastropods, and mammals. The enzymes isolated purified from chicken, Clostridium perfringens, rice and Elizabethkingia meningosepticum have been shown to efficiently cleave the terminal α-linked GalNAc from blood group A erythrocytes, resulting in a blood group H(O) epitope structure. An increasing interest on this enzyme was aroused by the use in biotechnology when the group H(O) “universal blood” was obtained by enzymatic conversion of A and AB donor blood.

Alpha-N-acetylgalactosaminidase from human tissue was initially considered to be an isoenzyme of α-galactosidase and thereafter was called α-galactosidase B. Patients with Fabry disease are deficient in α-galactosidase A activity, while the B form occurs at normal or even somewhat elevated levels in these patients. The two enzymes have similar physicochemical properties, the same subunit molecular mass, homodimeric structure, and similar amino acid compositions. However, subsequent kinetic, inhibitor, immunologic, and gene mapping studies demonstrated that α-galactosidase A and B are genetically distinct lysosomal enzymes with different substrate specificities, and that α-galactosidase B is, in reality, an alpha-N-acetylgalactosaminidase. Although the physiological function of alpha-N-acetylgalactosaminidase has not been well studied well, deficiency in lysosomal alpha-N-acetylgalactosaminidase, which causes autosomal recessive disorders, was reported and called Schindler disease and Kanzaki disease.

More detailed information, such as the molecular mechanism of action and kinetics of catalysis, is much desired due to the important roles of alpha-N-acetylgalactosaminidase in multiple biological processes. Therefore, further studies push a strong demand for accurately monitoring the enzyme activity of alpha-N-acetylgalactosaminidase. Creative Enzymes is fully prepared for highly standardized enzymatic assays for alpha-N-acetylgalactosaminidase. The activity of alpha-N-acetylgalactosaminidase is determined by the spectrophotometric assay. Our test results are the most trusted and proven, resulting in service requests that significantly grow in amount every year. Overall, Creative Enzymes is your best choice of enzyme activity measurement, and is well known to provide the best customer satisfaction.


The crystal structure of human alpha-N-acetylgalactosaminidase Figure: The crystal structure of human alpha-N-acetylgalactosaminidase.
PDB: 3H53



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