Activity of beta-galactosidase in homogenates and isolated microvilli fraction of jejunal mucosa from suckling rats.
1. beta-Galactosidase activity was studied in homogenates and isolated microvilli fraction of jejunal mucosa from 14-day-old suckling rats. o-Nitrophenyl beta-d-galactoside served as the substrate. 2. The microvilli fraction contains about one-third of the total activity of the original homogenate. 3. The pH optimum of the beta-galactosidase was 3.5 in the total homogenate and supernatant fraction, whereas in the microvilli fraction the maximum activity was at pH5.5. 4. This work gives further support to the view that two beta-galactosidases exist in the jejunal mucosa.
D000818:Animals; D005260:Female; D005696:Galactosidases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D007583:Jejunum / Q000201:enzymology*; D007774:Lactation; D009092:Mucous Membrane / Q000201:enzymology*; D011247:Pregnancy; D051381:Rats; D013347:Subcellular Fractions / Q000378:metabolism
D005696:Galactosidases