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

• About 70% of the DIDS-sensitive NAP-taurine binding sites are located in band 3, with the remainder largely in a lower molecular weight (band 4) region [5].
• This site is less than 51 A from the disulfonic stilbene binding site, as judged by fluorescence resonance energy transfer from BIDS to NAP-taurine [6].
• The mechanism also accounts for the enormous range of substrate structures accepted by the system, for the complex inhibition by the organic sulfate NAP-taurine, and for the involvement of several cationic side chains and two different protein domains in the transport site [7].

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

• NAP-taurine labeled all of the subunits of cytochrome c oxidase [12].
• It is shown that native ribonuclease A retains 90% of its enzymatic activity when flashed in the absence of NAP-Taurine [13].
• NAP-taurine inhibited the slice accumulation of PAH in a dose-dependent manner (ID50 = 2.5 X 10(-5) M) [14].
• Lys-539, a probable reaction site of BSSS, lies within the same segment of AE1 that is labeled by NAP-taurine and thus may be part of the modifier site [11].

References