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Why beta galactosidase has to be removed after insulin production? 

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This drop was due to a decrease in production of active beta-galactosidase rather than to inactivation of this enzyme.
Enzyme activity measurements in medium conditioned by genetically modified cells suggest that the human beta-galactosidase enzyme is less efficiently released to the extracellular space than its mouse counterpart.
Open accessJournal ArticleDOI
Michael D. Yudkin, V. Moses 
23 Citations
It is concluded that repression of beta-galactosidase synthesis can be brought about by the presence of glucose during the translation phase only.
From these studies, we show that multiple regions of beta-galactosidase contribute to its failure to be translocated.
The mild hyperglycemic action of galanin seems to be due to an inhibition of insulin production.
These results indicate that β-galactosidase activity plays an important role in malodor production.
Under these conditions, beta-galactosidase synthesis occurs at less than 1% of the rate obtained with unfractionated extracts, which suggested that other required components were lacking.
We conclude that the ebg beta-galactosidase may have arisen by modification of a gene involved with the metabolism of a monosaccharide, possibly a 2-amino sugar.

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