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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1971 Oct;68(10):2604–2607. doi: 10.1073/pnas.68.10.2604

Irreversible Inhibition of Biotin Transport in Yeast by Biotinyl-p-nitrophenyl Ester

Jeffrey M Becker 1, Meir Wilchek 1, Ephraim Katchalski 1
PMCID: PMC389477  PMID: 4944635

Abstract

Biotinyl-p-nitrophenyl ester (BNP), an active-ester derivative of biotin, irreversibly inactivates biotin transport in the yeast Saccharomyces cerevisiae. Transport inactivation is progressive with time and occurs at concentrations of the ester as low as 10-7 M. In the presence of sodium azide, a reagent known to block biotin accumulation in yeast, the derivative is still effective. The specificity of inactivation by the ester is revealed by the following findings: (a) Biotinyl-p-nitroanilide and acetyl-p-nitrophenyl ester do not affect biotin transport; (b) the nitrophenyl ester does not affect the transport of lysine and aspartic acid, or that of L-sorbose; (c) inactivation of biotin transport by the ester is partially prevented when the cells are incubated with it in the presence of relatively high concentrations of biotin.

Keywords: affinity label, biotinyl-p-nitroanilide, acetyl-p-nitrophenyl ester, sorbose transport, amino-acid transport

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Selected References

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

  1. Chavin S. I. Isolation and study of functional membrane proteins Present status and future prospects. FEBS Lett. 1971 May 20;14(5):269–282. doi: 10.1016/0014-5793(71)80278-8. [DOI] [PubMed] [Google Scholar]
  2. Fox C. F., Kennedy E. P. Specific labeling and partial purification of the M protein, a component of the beta-galactoside transport system of Escherichia coli. Proc Natl Acad Sci U S A. 1965 Sep;54(3):891–899. doi: 10.1073/pnas.54.3.891. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Kundig W., Roseman S. Sugar transport. I. Isolation of a phosphotransferase system from Escherichia coli. J Biol Chem. 1971 Mar 10;246(5):1393–1406. [PubMed] [Google Scholar]
  4. Pardee A. B. Membrane transport proteins. Proteins that appear to be parts of membrane transport systems are being isolated and characterized. Science. 1968 Nov 8;162(3854):632–637. doi: 10.1126/science.162.3854.632. [DOI] [PubMed] [Google Scholar]
  5. Rogers T. O., Lichstein H. C. Characterization of the biotin transport system in Saccharomyces cerevisiae. J Bacteriol. 1969 Nov;100(2):557–564. doi: 10.1128/jb.100.2.557-564.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Singer S. J. Covalent labeling of active sites. Adv Protein Chem. 1967;22:1–54. doi: 10.1016/s0065-3233(08)60040-6. [DOI] [PubMed] [Google Scholar]

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