2 results match your criteria e1ec

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The N-terminal 1-55 residues domain of pyruvate dehydrogenase from Escherichia coli assembles as a dimer in solution.

Protein Eng Des Sel 2019 12;32(6):271-276

College of Chemistry and Pharmacy, Northwest A&F University, Yangling, China.

The pyruvate dehydrogenase complex (PDHc) from Escherichia coli is a large protein complex consisting of multiple copies of the pyruvate dehydrogenase (E1ec), dihydrolipoamide acetyltransferase (E2ec) and dihydrolipoamide dehydrogenase (E3ec). The N-terminal domain (NTD, residues 1-55) of E1ec plays a critical role in the interaction between E1ec and E2ec and the whole PDHc activity. Using circular dichroism, size-exclusion chromatography and dynamic light scattering spectroscopy, we show that the NTD of E1ec presents dimeric assembly under physiological condition. Read More

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December 2019

Influence of restricted diet on epithelial renewal and maturation in the mice jejunum.

Authors:
A Koga S Kimura

J Nutr Sci Vitaminol (Tokyo) 1978 ;24(3):323-9

It has been known that the intestinal epithelial cell is characterized by a rapid cell turnover and by a gradient of differentiation from crypt to villus. The present study was undertaken to clarity the effect of diet on the migration and the maturation of the intestinal epithelial cells. The transit time from the crypt to the extrusion zone at the villus tip was determined with tritiated thymidine. Read More

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December 1978
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