AI Article Synopsis

  • Researchers studied acid and neutral beta-galactosidases from the intestinal mucosa of suckling rats, finding their characteristics and behaviors.
  • The acid beta-galactosidase had a molecular weight between 83,000-105,000, while the neutral type was significantly larger at 360,000-510,000.
  • Both enzymes showed competitive inhibition by certain compounds, with distinct K(i) values, and were inactivated by heat and urea, with the neutral enzyme being more sensitive.
  • No differences in enzyme properties were observed between the jejunum and ileum samples.

Article Abstract

1. The characteristics of acid and neutral beta-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 beta-galactosidase, as estimated by gel filtration on Sephadex G-200, was in the range 83000-105000, whereas for the neutral beta-galactosidase the estimated molecular weight was in the range 360000-510000. 3. The acid and neutral beta-galactosidases were inhibited competitively by galactono-(1-->4)-lactone, with respective K(i) values of 0.15mm and 1.1mm. Only the acid beta-galactosidase was inhibited competitively by sodium galactonate (K(i) 0.17mm). 4. Heat inactivation of both beta-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 beta-galactosidases, the neutral beta-galactosidase being more sensitive than the acid beta-galactosidase. 6. No differences were found between preparations from the jejunum and ileum.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1184935PMC
http://dx.doi.org/10.1042/bj1140621DOI Listing

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