Literature DB >> 4980717

o-Quinones formed in plant extracts. Their reaction with bovine serum albumin.

W S Pierpoint.   

Abstract

1. The reactions between chlorogenoquinone, the o-quinone formed during the oxidation of chlorogenic acid, and bovine serum albumin depend on the ratio of reactants. 2. When the serum albumin is in excess, oxygen is not absorbed and the products are colourless. This reaction probably involves the thiol group of bovine serum albumin; it does not occur with bovine serum albumin which has been treated with p-chloromercuribenzoate, iodoacetamide or Ellman's reagent. 3. When bovine serum albumin reacts with excess of chlorogenoquinone, oxygen is absorbed and the products are red. The red colour is probably formed by reaction of the lysine in-amino groups of bovine serum albumin, as it is prevented by treating the protein with formaldehyde, succinic anhydride or O-methylisourea. 4. Bovine serum albumin modified by a 1.5-fold (BSA-Q) and a fivefold (BSA-Q2) excess of chlorogenoquinone were separated by chromatography on DEAE-Sephadex A-50, and some of their properties observed. 5. Reaction of BSA-Q2 with fluorodinitrobenzene suggests that the terminal alpha-amino group, as well as lysine in-amino groups, are combined with chlorogenoquinone.

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Year:  1969        PMID: 4980717      PMCID: PMC1187765          DOI: 10.1042/bj1120619

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  14 in total

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7.  The enzymic oxidation of chlorogenic acid and some reactions of the quinone produced.

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8.  The heterogeneity of bovine serum albumin.

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10.  o-Quinones formed in plant extracts. Their reactions with amino acids and peptides.

Authors:  W S Pierpoint
Journal:  Biochem J       Date:  1969-05       Impact factor: 3.857

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10.  o-Quinones formed in plant extracts. Their reactions with amino acids and peptides.

Authors:  W S Pierpoint
Journal:  Biochem J       Date:  1969-05       Impact factor: 3.857

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