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. 1969 Sep;114(3):621–627. doi: 10.1042/bj1140621

Characteristics of β-galactosidase in the mucosa of the small intestine of infant rats. Physicochemical properties

Jiří Kraml 1, Otakar Koldovský 1, Aleša Heringová 1, Věra Jirsová 1, Karel Kácl 1, Miloš Ledvina 1, Hana Pelichová 1
PMCID: PMC1184935  PMID: 5820646

Abstract

1. The characteristics of acid and neutral β-galactosidases isolated chromatographically from homogenates of the mucosa of the jejunum and ileum of suckling rats were studied. 2. The minimal molecular weight of the acid β-galactosidase, as estimated by gel filtration on Sephadex G-200, was in the range 83000–105000, whereas for the neutral β-galactosidase the estimated molecular weight was in the range 360000–510000. 3. The acid and neutral β-galactosidases were inhibited competitively by galactono-(1→4)-lactone, with respective Ki values of 0·15mm and 1·1mm. Only the acid β-galactosidase was inhibited competitively by sodium galactonate (Ki 0·17mm). 4. Heat inactivation of both β-galactosidases occurred according to first-order kinetics. The neutral enzyme was more labile, but bovine serum albumin protected acid enzyme only. 5. Urea treatment inactivated both β-galactosidases, the neutral β-galactosidase being more sensitive than the acid β-galactosidase. 6. No differences were found between preparations from the jejunum and ileum.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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