Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1973 Sep;135(1):59–61. doi: 10.1042/bj1350059

Effect of high tyrosine content on the determination of tryptophan in protein by the acidic ninhydrin method. Application to chicken ovoinhibitor

James C Zahnley 1, John Gorton Davis 1
PMCID: PMC1165788  PMID: 4798181

Abstract

Colorimetric determination of tryptophan in intact proteins by the acidic ninhydrin method of Gaitonde & Dovey (1970) gives high apparent tryptophan contents for proteins having high tyrosine/tryptophan ratios. Correction for this interference by tyrosine can be achieved by plotting the ratio of observed to expected tryptophan content as a function of tyrosine/tryptophan ratio for proteins of known composition. The equation of the line is: [Formula: see text] Application of this correction to chicken ovoinhibitor, which contains 17 tyrosine residues per molecule, gave results that agree with tryptophan content determined by other methods.

Full text

PDF
59

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Barth G., Bunnenberg E., Djerassi C. Magnetic circular dichroism studies. XIX. Determination of the tyrosine: tryptophan ratio in proteins. Anal Biochem. 1972 Aug;48(2):471–479. doi: 10.1016/0003-2697(72)90100-5. [DOI] [PubMed] [Google Scholar]
  2. Barth G., Voelter W., Bunnenberg E., Djerassi C. Magnetic circular dichroism studies. XVII. Magnetic circular dichroism spectra of proteins. A new method for the quantitative determination of tryptophan. J Am Chem Soc. 1972 Feb 23;94(4):1293–1298. doi: 10.1021/ja00759a041. [DOI] [PubMed] [Google Scholar]
  3. Davis J. G., Mapes C. J., Donovan J. W. Batch purification of ovomucoid and characterization of the purified product. Biochemistry. 1971 Jan 5;10(1):39–42. doi: 10.1021/bi00777a006. [DOI] [PubMed] [Google Scholar]
  4. Davis J. G., Zahnley J. C., Donovan J. W. Separation and characterization of the ovoinhibitors from chicken egg white. Biochemistry. 1969 May;8(5):2044–2053. doi: 10.1021/bi00833a039. [DOI] [PubMed] [Google Scholar]
  5. Friedman M., Finley J. W. Methods of tryptophan analysis. J Agric Food Chem. 1971 Jul-Aug;19(4):626–631. doi: 10.1021/jf60176a010. [DOI] [PubMed] [Google Scholar]
  6. Gaitonde M. K., Dovey T. A rapid and direct method for the quantitative determination of tryptophan in the intact protein. Biochem J. 1970 May;117(5):907–911. doi: 10.1042/bj1170907. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Liu W. H., Means G. E., Feeney R. E. The inhibitory properties of avian ovoinhibitors aganist proteolytic enzymes. Biochim Biophys Acta. 1971 Jan 19;229(1):176–185. doi: 10.1016/0005-2795(71)90331-x. [DOI] [PubMed] [Google Scholar]
  8. Tomimatsu Y., Clary J. J., Bartulovich J. J. Physical characterization of ovoinhibitor, a trypsin and chymotrypsin inhibitor from chicken egg white. Arch Biochem Biophys. 1966 Sep 9;115(3):536–544. doi: 10.1016/0003-9861(66)90073-7. [DOI] [PubMed] [Google Scholar]
  9. Zahnley J. C., Davis J. G. Determiniation of trypsin-inhibitor complex dissociation by use of the active site titrant, p-nitrophenyl p'-guanidinobenzoate. Biochemistry. 1970 Mar 17;9(6):1428–1433. doi: 10.1021/bi00808a018. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES