Journal
APPLIED BIOCHEMISTRY AND MICROBIOLOGY
Volume 46, Issue 3, Pages 297-302Publisher
PLEIADES PUBLISHING INC
DOI: 10.1134/S0003683810030087
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Funding
- Russian Foundation for Basic Research [09-04-01286-a, 09-04-01674-a]
- Federal Agency for Science and Innovations [02.512.11.2254]
- Science and Science Education Staff for Innovative Russia Federal Target Program [P808, P1201]
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A nonenzymatic glycation of the recombinant leghemoglobin expressed in Escherichia coli cells was demonstrated for the first time. This process involved the heme pocket and gave low-spin leghemoglobin species. A correlation between the degree of E. coli protein glycation and synthesis of poly-beta-hydroxybutyric acid was found, suggesting that the accumulation of reserve carbon sources and nonenzymatic glycation could be alternative processes.
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