[Formation of glycated recombinant leghemoglobin in Escherichia coli cells].
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.
Kosmachevskaia
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OV
Topunov
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D004926:Escherichia coli; D015870:Gene Expression; D006031:Glycosylation; D007874:Leghemoglobin / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics; D011994:Recombinant Proteins / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics; D013025:Glycine max
D007874:Leghemoglobin; D011994:Recombinant Proteins