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Chemical Compound Review

NAP taurine     2-[(4-azido-2-nitro- phenyl)amino]ethanesul...

Synonyms: AC1MC3AY, 57462-29-0, 2-(4-azido-2-nitroanilino)ethanesulfonic acid
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High impact information on NAP taurine

  • Addition of DNDS (4,4'-dinitrostilbene-2,2'-disulfonate), protects PLP labeling of CH35 but exposes new, nonoverlapping sites on CH17.4,4'-Diisothiocyanostilbene-2,2'-disulfonate reduces PLP labeling to both domains with time, while NAP-taurine (N(-4-azido-2-nitrophenyl)2-aminosulfonate) has no effect on either domain [1].
  • N-(4-Azido-2-nitrophenyl)-2-aminoethylsulfonate, a reversible noncompetitive inhibitor of anion transport did not protect against EAC inhibition of transport but prevented reversal of inhibition in saline medium [2].
  • These results indicate that 7-ADTC and NAP-taurine can be utilized as photoaffinity probes for the identification of the bile acid carrier protein(s) in hepatocyte plasma membranes [3].
  • The transport properties of the photoreactive anion transport inhibitor, N-(4-azido-2-nitrophenyl)-2-aminoethylsulfonate (NAP-taurine) were also characterized in the hepatocyte system [3].
  • Selective antagonism of the Ca2+ transport ATPase of the red cell membrane by N-(14-azido-2-nitrophenyl)-2-aminoethylsulfonate (NAP-taurine) [4].

Biological context of NAP taurine


Anatomical context of NAP taurine

  • N-(4-azido-2-nitrophenyl)-2-aminoethyl sulfonate (NAP-taurine), a photolabile nitrene precursor, has been shown to permeate the human erythrocyte membrane at 37degrees but not at 0 degrees [8].
  • The number of anion transport sites available on the cytoplasmic side of the vesicle membranes was then estimated by measuring the binding of N-(-4-azido-2-nitrophenyl)-2-aminoethyl-sulfonate (NAP-taurine), a photoreactive probe [5].
  • The present investigation compares brush-border (BBM) and basolateral membrane (BLM) vesicles in terms of purity, function, appearance on sodium dodecyl sulfate (SDS) gels, and labeling pattern by use of N-(4-azido-2-nitrophenyl)-2-aminoethanesulfonic acid (NAP-taurine), a photoaffinity analogue of p-aminohippurate (PAH) [9].

Associations of NAP taurine with other chemical compounds

  • A Ca-stimulated ATPase activity (pH 9.5) associated with the tegumental membrane enriched (TME) fraction of Schistosoma mansoni adults was partially inhibited by NAP-taurine or by increasing concentrations of chlorpromazine; endogenous calmodulin was found associated with the TME fraction [10].
  • NIP- and NAP-taurine bind to external modifier site of AE1 (band 3), at which iodide inhibits anion exchange [11].

Gene context of NAP taurine


  1. Characterization of pyridoxal 5'-phosphate affinity labeling of band 3 protein. Evidence for allosterically interacting transport inhibitory subdomains. Salhany, J.M., Rauenbuehler, P.B., Sloan, R.L. J. Biol. Chem. (1987) [Pubmed]
  2. Reversible and irreversible inhibition of phosphate transport in human erythrocytes by a membrane impermeant carbodiimide. Craik, J.D., Reithmeier, R.A. J. Biol. Chem. (1985) [Pubmed]
  3. Synthesis and transport characteristics of photoaffinity probes for the hepatocyte bile acid transport system. von Dippe, P., Drain, P., Levy, D. J. Biol. Chem. (1983) [Pubmed]
  4. Selective antagonism of the Ca2+ transport ATPase of the red cell membrane by N-(14-azido-2-nitrophenyl)-2-aminoethylsulfonate (NAP-taurine). Minocherhomjee, A., Roufogalis, B.D. J. Biol. Chem. (1982) [Pubmed]
  5. Transmembrane effects of irreversible inhibitors of anion transport in red blood cells. Evidence for mobile transport sites. Grinstein, S., McCulloch, L., Rothstein, A. J. Gen. Physiol. (1979) [Pubmed]
  6. Mechanism of anion exchange across the red cell membrane by band 3: interactions between stilbenedisulfonate and NAP-taurine binding sites. Macara, I.G., Cantley, L.C. Biochemistry (1981) [Pubmed]
  7. Role of substrate binding forces in exchange-only transport systems: II. Implications for the mechanism of the anion exchanger of red cells. Krupka, R.M. J. Membr. Biol. (1989) [Pubmed]
  8. Photochemical labeling of the cytoplasmic surface of the membranes of intact human erythrocytes. Staros, J.V., Richards, F.M. J. Biol. Chem. (1975) [Pubmed]
  9. Photoaffinity labeling of organic anion transport system in proximal tubule. Goldinger, J.M., Khalsa, B.D., Hong, S.K. Am. J. Physiol. (1984) [Pubmed]
  10. Tegumental Ca-stimulated adenosine triphosphatase activity in adult Schistosoma mansoni worms. Cesari, I.M., Aldana, E., Gil, F., Condrescu, M. Mem. Inst. Oswaldo Cruz (1989) [Pubmed]
  11. NIP- and NAP-taurine bind to external modifier site of AE1 (band 3), at which iodide inhibits anion exchange. Knauf, P.A., Spinelli, L.J. Am. J. Physiol. (1995) [Pubmed]
  12. Structure of the cytochrome c oxidase complex: labeling by hydrophilic and hydrophobic protein modifying reagents. Prochaska, L., Bisson, R., Capaldi, R.A. Biochemistry (1980) [Pubmed]
  13. Study of protein topography with flash photolytically generated nonspecific surface-labeling reagents: surface labeling of ribonuclease A. Matheson, R.R., Van Wart, H.E., Burgess, A.W., Weinstein, L.I., Scheraga, H.A. Biochemistry (1977) [Pubmed]
  14. Renal transport of NAP-taurine. Stokols, M.F., Koschier, F.J., Goldinger, J.M., Hong, S.K. Am. J. Physiol. (1981) [Pubmed]
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