Literature DB >> 5117027

The cross-linking of tyrosine by treatment with tetranitromethane.

J Williams, J M Lowe.   

Abstract

1. Tyrosine was treated with tetranitromethane. 2. Approx. 10% of the tyrosine was converted into 3-nitrotyrosine. 3. Three fluorescent compounds were also formed. They appear to be a dimer, trimer and tetramer in which tyrosine units are linked by biphenyl bonds. 4. The dimer and trimer have also been isolated from some proteins after treatment with tetranitromethane. 5. The yield of 3-nitrotyrosine from ovotransferrin after treatment with tetranitromethane was much smaller than the loss of tyrosine. 6. Several unidentified compounds were also formed by the reaction between tyrosine and tetranitromethane.

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Year:  1971        PMID: 5117027      PMCID: PMC1176556          DOI: 10.1042/bj1210203

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


  11 in total

1.  [Amino acid determination on paper chromatograms].

Authors:  J HEILMANN; J BARROLLIER; E WATZKE
Journal:  Hoppe Seylers Z Physiol Chem       Date:  1957

2.  Multiple dipping procedures in paper chromatography: a specific test for hydroxy-proline.

Authors:  J B JEPSON; I SMITH
Journal:  Nature       Date:  1953-12-12       Impact factor: 49.962

3.  The preparation of crystalline conalbumin.

Authors:  R C WARNER; I WEBER
Journal:  J Biol Chem       Date:  1951-07       Impact factor: 5.157

4.  Probable protein crosslinking with tetranitromethane.

Authors:  R J Doyle; J Bello; O A Roholt
Journal:  Biochim Biophys Acta       Date:  1968-06-26

5.  Enzymic and immunochemical properties of lysozyme. I. Derivatives modified at tyrosine. Influence of nature of modification on activity.

Authors:  M Z Atassi; A F Habeeb
Journal:  Biochemistry       Date:  1969-04       Impact factor: 3.162

6.  Tetranitromethane. A reagent for the nitration of tyrosyl residues in proteins.

Authors:  M Sokolovsky; J F Riordan; B L Vallee
Journal:  Biochemistry       Date:  1966-11       Impact factor: 3.162

7.  On the use of tetranitromethane as a nitration reagent. The reaction of phenol side-chains in bovine and porcine trypsinogens and trypsins.

Authors:  J P Vincent; M Lazdunski; M Delaage
Journal:  Eur J Biochem       Date:  1970-02

8.  Crosslinking during the nitration of bovine insulin with tetranitromethane.

Authors:  R W Boesel; F H Carpenter
Journal:  Biochem Biophys Res Commun       Date:  1970-02-20       Impact factor: 3.575

9.  Electrophoretic mobilities of peptides on paper and their use in the determination of amide groups.

Authors:  R E Offord
Journal:  Nature       Date:  1966-08-06       Impact factor: 49.962

10.  A comparison of glycopeptides from the ovotransferrin and serum transferrin of the hen.

Authors:  J Williams
Journal:  Biochem J       Date:  1968-06       Impact factor: 3.857

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  6 in total

1.  The cross-linking of tyrosine residues in apo-ovotransferrin by treatment with periodate anions.

Authors:  J J Hsuan
Journal:  Biochem J       Date:  1987-10-15       Impact factor: 3.857

2.  Mushroom tyrosinase oxidizes tyrosine-rich sequences to allow selective protein functionalization.

Authors:  Marcus J C Long; Lizbeth Hedstrom
Journal:  Chembiochem       Date:  2012-07-17       Impact factor: 3.164

3.  (2-(3-Nitrotyrosine))oxytocin, a wealky activity analogue of the hormone bound by neurophysin.

Authors:  D B Hope; M Wálti
Journal:  Biochem J       Date:  1973-09       Impact factor: 3.857

Review 4.  Contact-site cross-linking agents.

Authors:  G R Kunkel; M Mehrabian; H G Martinson
Journal:  Mol Cell Biochem       Date:  1981-01-20       Impact factor: 3.396

5.  Preferential nitration with tetranitromethane of a specific tyrosine residue in penicillinase from Staphylococcus aureus PCl. Evidence that the preferentially nitrated residue is not part of the active site but that loss of activity is due to intermolecular cross-linking.

Authors:  A F Bristow; R Virden
Journal:  Biochem J       Date:  1978-02-01       Impact factor: 3.857

6.  Formation of dityrosine and other fluorescent amino acids by reaction of amino acids with lipid hydroperoxides.

Authors:  K Kikugawa; T Kato; A Hayasaka
Journal:  Lipids       Date:  1991-11       Impact factor: 1.880

  6 in total

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