Japanese Journal of Clinical Chemistry
Online ISSN : 2187-4077
Print ISSN : 0370-5633
ISSN-L : 0370-5633
Anomeric Preference of Maltose Hydrolysis by the Brush Border-Bound Maltase from the Rat Small Intestine
KAZUO MAEDAICHITOMO MIWAJUN OKUDA
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1982 Volume 11 Issue 3 Pages 194-199

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Abstract
The Km value (0.ssmM) of the brush border-bound maltase from the rat small intestine for a-maltose was lower than that (2.3mM) for β-maltose, whereas the Vmax values for both anomers were the same. Thus, at finite concentrations, α-maltose was better hydrolyzed than β-maltose by the enzyme. This α-anomeric preference seemed to be purposive in starch digestion because pancreatic α-amylase is known to produce maltose in the a form from starch. A modification, utilizing fluorometry of NADH, of a spectrophotometric method for the assay of glucose anomers with β-D-glucose dehydrogenase and mutarotase was developed and applied to the anomer analysis of the glucose released by hydrolysis of maltose by the brush border-bound maltase. The glucose of the non-reducing end was released exclusively in the a form: i.e., almost entirely pure a-Dglucose was produced from a-maltose. The data obtained in this study were discussed in relation to the transport mechanism of the glucose liberated from maltose.
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