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- W2079353213 abstract "Biotinidase was purified from human breast milk (4 000-fold), and was compared with human serum biotinidase (enriched 30 000-fold). The molecular weight of milk enzyme was 68 000 Da is determined by SDS-PAGE. It was definitely smaller than that of serum biotinidase (Mr = 76 000). Isoelectric point of milk biotinidase was 4.6, whereas that of serum biotinidase was 4.3. Sialic acid pontent in milk biotinidase was less than that found in serum enzyme. N-Acetyl-galactosamine was present in milk enzyme, whereas it was absent in serum enzyme. Milk biotinidase is O-glycosylated, thereas serum biotinidase is N-glycosylated. These differences in glycosylation suggest the existence of different types of excretion mechanisms between milk and serum biotinidase. Both biotinidases were found to be thiol-type enzyme, however, the extent of activation of the enzemy 2-mercaptoethanol was 13-fold in milk, whilt the serum enzyme was activated only 1.5-fold. Km for biotinyl-4-amino-benzoate was 22 μM in milk enzyme and 50 μM in seruum enzyme. Competitive inhibition by biotin (Ki) of milk enzyme was 43 μM and 1.3 mM for serum enzyme. These results suggeest the structural differences it or near the active site of the each enzyme." @default.
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- W2079353213 date "1989-11-01" @default.
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- W2079353213 title "Comparative study of human milk and serum biotinidase" @default.
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- W2079353213 doi "https://doi.org/10.1016/0300-9084(89)90019-9" @default.
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