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-β-hydr...

Full description

Saved in:
Bibliographic Details
Published in:Applied biochemistry and microbiology 2010-05, Vol.46 (3), p.297-302
Main Authors: Kosmachevskaya, O. V, Topunov, A. F
Format: Article
Language:English
Subjects:
Biochemistry
Biomedical and Life Sciences
Carbon sources
Cellular biology
E coli
Escherichia coli
Genetic recombination
Life Sciences
Medical Microbiology
Microbiology
Proteins
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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-β-hydroxybutyric acid was found, suggesting that the accumulation of reserve carbon sources and nonenzymatic glycation could be alternative processes.
ISSN:0003-6838
1608-3024
DOI:10.1134/S0003683810030087