INTESTINAL DIGESTION AND ABSORPTION OF SUGARS AND PEPTIDES.
Final scientific rept. 1 Dec 66-31 Dec 67,
ZURICH UNIV (SWITZERLAND) BIOCHEMISCHES INSTITUT
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The allosteric properties of sucrase were investigated. There is an evident homologous interaction between Na-sites and between substrate-sites. Large species differences are present. The reaction sequence is non-compulsory. The Na-sites do not contain easily accessible phenol- or SH-group Sucrase, which has no mutarotase activity, liberates glucose in its alpha form. The beta forms of glucose and of some of its derivatives are absorbed preferentially. Human and rabbit intestinal sucrases were isolated. Antibodies against them were prepared. A new procedure for the measurement of intestinal uptake was developed. It allows the determination of unidirectional flow. Rat intestinal lactase was isolated it is not activated by Na. Pancreatic amylase sets free the alpha-form of maltose, as determined by gas chromatography. A procedure for the determination of sugar uptake in human peroral biopsies was developed. Author