(Q77149539)

English

Reactivity of 6-phosphogluconolactone with hydroxylamine: the possible involvement of glucose-6-phosphate dehydrogenase in endogenous glycation reactions

scientific article published on 01 June 1998

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scholarly article

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3 December 2019

Reactivity of 6-phosphogluconolactone with hydroxylamine: the possible involvement of glucose-6-phosphate dehydrogenase in endogenous glycation reactions (English)

1 reference

Europe PubMed Central

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3 December 2019

author name string

E T Rakitzis

1

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3 December 2019

P Papandreou

2

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publication date

1 June 1998

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3 December 2019

Chemico-biological Interactions

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3 December 2019

113

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3 December 2019

205-216

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3 December 2019

3

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3 December 2019

A New N-Terminal Blocking Group Involving a Schiff Base in Hemoglobin AIc*

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RATES OF HYDROLYSIS AND INTERACTION WITH CYSTEINE OF SOME CARCINOGENIC LACTONES AND RELATED SUBSTANCES

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THE REACTION OF BETA-PROPIOLACTONE WITH GUANOSINE, DEOXYGUANYLIC ACID AND RNA

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Reaction of β-propiolactone with amino acids and its specificity for methionine

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In vitro reaction of β-propiolactone and γ-butyrolactone with glutathione and cysteine

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Reversibility of glucose-6-phosphate oxidation

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Purification and properties of acyl phosphatase from human erythrocytes.

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Kinetic analysis of chemical or enzymic reactions: an algorithm for the determination of the initial velocity of product formation by the use of a taylor series in reaction time.

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Transformation and Hydrolysis of D-Glucono-γ and δ-Lactone

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Nature of primary product(s) of D-glucose 6-phosphate dehydrogenase reaction. 13C and 31P NMR study

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Regulation of the human-erythrocyte hexose-monophosphate shunt under conditions of oxidative stress. A study using NMR spectroscopy, a kinetic isotope effect, a reconstituted system and computer simulation

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6-Phosphogluconolactonase deficiency, a hereditary erythrocyte enzyme deficiency: possible interaction with glucose-6-phosphate dehydrogenase deficiency

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A new acylphosphatase isoenzyme from human erythrocytes: purification, characterization, and primary structure

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Hexose monophosphate shunt enzymes in lung tumors from normal and glucose-6-phosphate-dehydrogenase-deficient subjects

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10.1016/S0009-2797(98)00026-X

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Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9717519%20AND%20SRC:MED&resulttype=core&format=json

3 December 2019

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9717519%20AND%20SRC:MED&resulttype=core&format=json

3 December 2019

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