The irreversible combination of formaldehyde with proteins

Middlebrook, W. R.

doi:10.1042/bj0440017

Cited by 19 publications

(7 citation statements)

References 21 publications

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“…In competition experiments, where 1 equivalent of HCHO was added to reaction mixtures containing Cys and either Thr, Hse, Asn, His, Trp, Arg, Lys, or Orn (1:1 ratio), exclusive formation of Cys derived thiazolidine 1 was observed within 12 h; with the exception of His, no other products were observed during this time period (Supplementary Figs. [26][27][28][29][30][31][32][33][34]. With His, N,N-cyclised 17 was observed initially, but this product reverted to His alongside the formation of thiazolidine 1 over 5 h. We then conducted competition experiments with the three thiol-containing AAs, Cys, Hcy and Pen.…”

Section: Resultsmentioning

confidence: 99%

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How formaldehyde reacts with amino acids

et al. 2019

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Formaldehyde is a biological electrophile produced via processes including enzymatic demethylation. Despite its apparent simplicity, the reactions of formaldehyde with even basic biological components are incompletely defined. Here we report NMR-based studies on the reactions of formaldehyde with common proteinogenic and other nucleophilic amino acids. The results reveal formaldehyde reacts at different rates, forming hydroxymethylated, cyclised, cross-linked, or disproportionated products of varying stabilities. Of the tested common amino acids, cysteine reacts most efficiently, forming a stable thiazolidine. The reaction with lysine is less efficient; low levels of an Nε-methylated product are observed, raising the possibility of non-enzymatic lysine methylation by formaldehyde. Reactions with formaldehyde are faster than reactions with other tested biological carbonyl compounds, and the adducts are also more stable. The results reveal reactions of formaldehyde with amino acids, and by extension peptides and proteins, have potential roles in healthy and diseased biology, as well as in evolution.

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Section: Resultsmentioning

confidence: 99%

“…Following pioneering work in the 1920s, numerous studies have been reported on reactions of HCHO with amino acids (AAs) and peptides [24][25][26][27][28][29][30][31][32][33][34][35][36][37][38] . However, few detailed systematic studies have been reported on reactions of HCHO with amino acids.…”

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confidence: 99%

How formaldehyde reacts with amino acids

et al. 2019

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“…The tyrosine content of virgin wool fibres has been determined by various workers, the values obtained ranging from 4-5 to 5.8%. Marston (1928) found a value of 4-8%; Block (1937), 4.5%; Block (1939), 4.8%;Rutherford et al (1940), 5.8% and Middlebrook (1949), 5.43%. These workers used either the method of Thomas (1944) or some modification of the Millon reaction.…”

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confidence: 94%

The reaction of oxidizing agents with wool. 4. The reactivity of tyrosine

Alexander

Gough

1951

Biochemical Journal

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“…The pioneer descriptions of French et al (French andEdsall, 1945), Fraenkel-Conrat (Fraenkel-Conrat andMecham, 1949) and Middlebrook (Middlebrook, 1949) in the mid 1940's are some of the most comprehensive.…”

Section: Protein Modifications Induced By For-maldehyde Fixationmentioning

confidence: 97%

Proteomic Analysis of Formalin-Fixed Paraffin Embedded (FFPE) Samples: Pitfalls and Potentials

Valera¹,

Walter²,

Linehan³

et al. 2009

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Proteomic analysis of clinical samples has been traditionally performed using fresh or frozen tissues. However, millions of embedded samples are stored worldwide in pathology repositories with linked long-term outcome data. Such samples are believed to be unsuitable for proteome analysis because of the extensive protein modification attained during tissue processing. Formaldehyde, in the form of buffered formalin, is the most commonly used fixative during processing before embedding in paraffin. These formalin-fixed paraffin embedded (FFPE) tissue samples are widely used in pathology labs for qualitative protein analysis using immunohistochemistry (IHC). For this purpose, FFPE tissues are treated in different ways in order to reverse chemical modifications by formaldehyde that limit protein antigen detection by specific antibodies. Accordingly, intensive research efforts are now attempting to adapt the sample pretreatments used in immunohistochemistry to facilitate high throughput proteome analysis of FFPE tissues. Two such approaches have been successful: a liquid-based proteomic approach and an in situ approach, mainly based on separation and identification technologies such as liquid chromatography and mass spectrometry. These efforts have proven that similar protein profiles and numbers of polypeptides can be attained as using frozen sections. In this article, a review is provided of methods and current trends for the extraction of peptides and proteins from FFPE tissues for use proteomic analysis. Limitations in these methods and future directions to overcome these are also outlined. Ongoing improvements in protein extraction technology and analysis techniques will enable identification of novel disease biomarkers from FFPE tissues.

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The irreversible combination of formaldehyde with proteins

Cited by 19 publications

References 21 publications

How formaldehyde reacts with amino acids

How formaldehyde reacts with amino acids

The reaction of oxidizing agents with wool. 4. The reactivity of tyrosine

Proteomic Analysis of Formalin-Fixed Paraffin Embedded (FFPE) Samples: Pitfalls and Potentials

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