Authors
Abstract
Background and Purpose: Human serum a-mannosidase is important in glycoprotein and glycolipids processes for isolating the mannose link to protein and lipid. This is because glycoprotein and glycolipids are used in (nervous) cell membrane. Its deficiency causes psychiatric diseases. The present study was conducted to purify the human serum a-mannosidase in order to compare it with other human serum isoenzymes so that the results are used in future studies.
Methods and Materials: Human serum a-mannosidase was purified by gel filtration on sephadex G200 and affinity chromatography on Con-A CL seralose.
Results: a-mannosidase was purified 1384.6 times. The obtained molecular mass by gel filtration and electrophoresis (pH=8.3) were 354813 and 423790 Dal respectively. Carbohydrate amount was 10.6%. It was observed that the optimum pH and temperature for the enzyme were 4.2 and 40°c respectively. Respective Km value for a-mannosidase was 27.5 mM for p-nitrophenyl a-D-mannopyranoside. It was also discovered that Vmax was 101 unit per minute per mM of the enzyme substrate.
Conclusion: Purified a-mannosidase is different from other human serum isoenzymes due to its molecular mass and other enzymatic features.
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