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Pyruvic acid and acetaldehyde production by different strains of Saccharomyces cerevisiae: relationship with Vitisin A and B formation in red wines.

The production of pyruvate and acetaldehyde by 10 strains of Saccharomyces cerevisiae was monitored during the fermentation of Vitis vinifera L. variety Tempranillo grape must to determine how these compounds might influence the formation of the pyroanthocyanins vitisin A and B (malvidin-3-O-glucoside-pyruvate acid and malvidin-3-O-glucoside-4 vinyl, respectively). Pyruvate and acetaldehyde production patterns were determined for each strain. Pyruvate production reached a maximum on day four of fermentation, while acetaldehyde production was at its peak in the final stages. The correlation between pyruvate production and vitisin A formation was especially strong (R (2) = 0.80) on day 4, when the greatest quantity of pyruvate was found in the medium. The correlation between acetaldehyde production and the formation of vitisin B was strongest (R (2) = 0.81) at the end of fermentation when the acetaldehyde content of the medium was at its highest. Identification and quantification experiments were performed by HPLC-DAD. The identification of the vitisins was confirmed by LC/ESI-MS.

Acetaldehyde↗

Pyruvic acid is attached through its central carbon atom to the amino terminus of the recombinant DNA-derived DNA-binding protein Ner of bacteriophage Mu.

Ner protein of bacteriophage Mu, produced by recombinant DNA techniques in Escherichia coli, has been found to possess a molecule of pyruvic acid attached covalently through carbon-2 to the amino-terminal cysteine residue. The intact protein and the amino-terminal chymotryptic peptide were found by mass spectrometry to be 70 mass units heavier than expected. The modified peptide was unstable under mildly acid or mildly basic conditions. Two-dimensional nuclear magnetic resonance spectroscopy of the modified and unmodified forms of the amino-terminal chymotryptic peptide was consistent with the presence of pyruvate linked through carbon-2 to the amino-terminal Cys residue. Treatment of the modified form with 2,4-dinitrophenylhydrazine in acid medium led to the expected hydrazone of pyruvic acid, which was identified by high pressure liquid chromatography. Of the two proteins known to be modified by pyruvate through its central carbon (the other being human adult hemoglobin, in which the modified form represents only a very minor fraction), Ner is the first protein found to be modified quantitatively. Given the instability of the modification, it may be more prevalent than recognized hitherto. Incubation with 2,4-dinitrophenylhydrazine may offer a useful means of detecting the presence of pyruvate linked to proteins in this way.

Amino Acid Sequence↗

[Experimental study of the viability of warm ischemic kidney. Relationship between ATP value in renal tissue by isotachophoresis and serum pyruvic acid to lactic acid ratio (P/L ratio)].

The viability of preserved kidney is considered to be evaluated by mitochondrial function. We used the three experimental conditions of WIT 60 minutes (group I), 90 minutes (group II), and 120 minutes (group III) using rabbit. We measured the ATP value of renal tissue as a direct method before ischemia (control), immediately before recirculation, and at one hour, two hours, one day, two days, four days and seven days after recirculation, using isotachophoresis (Tachophor LKB 2127), and as an indirect method, serum pyruvic acid, lactic acid and LDH values were measured simultaneously. The ATP value in groups I, II, and III before recirculation were 1/10 lower than controls. However, as WIT became longer, the recovery speed was diminished. The serum P/L ratio reflected the mitochondrial function in group III. (p less than 0.05) The measurement of ATP value by this method, although it is somewhat invasive, is a useful method with a simple technique and a short analysis time. The serum P/L ratio is considered not to reflect the mitochondrial function directly, but can be measured adequately in WIT 120 minutes.

Adenosine Triphosphate↗

[Localization of pyruvic acid in the histidine decarboxylase of Micrococcus sp. n].

A fragment containing the pyruvic acid residue is isolated from hymotryptic hydrolyzate of alpha-polypeptide chain of carboxymethylated histidine decarboxylase (HD) 14C-phenylhydrasone. The pyruvate residue is estimated to be bind with alpha-amino group of N-terminal phenylalanine in alpha-polypeptide chain. N-terminal alanine is found in HD alpha-polypeptide chain after its reductive amination. It makes possible to determine the estimation of N-terminal amino acid sequence in HD alpha-chain.

Carboxy-Lyases↗