1976
DOI: 10.1111/j.1432-1033.1976.tb10228.x
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Fluorescence of Proteins in 6‐M Guanidine Hydrochloride

Abstract: To determine the tryptophan content in proteins, an analytical ultraviolet fluorescence method is proposed based on making uniform the environment of aromatic chromophores in 6 -7 M guanidine hydrochloride.The fluorescence intensity scale is calibrated using standard solutions of free tryptophan. A correlation coefficient between the fluorescence of protein tryptophanyl residues and of free tryptophan was estimated in testing 17 well characterized proteins.This method is particularly suited to proteins carryin… Show more

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Cited by 207 publications
(94 citation statements)
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“…Table 1 shows a comparison of the amino acid composition derived from the nucleotide sequence and that determined by amino acid analysis [31]. The agreement is very good, the exception being tryptophan which was determined by the fluorometric method of Pajot [32]. The presence of a single tryptophan (Trp199) is of interest because it may serve as a reporter group in fluorometric studies as it is located in the presumed NAD binding domain.…”
mentioning
confidence: 79%
“…Table 1 shows a comparison of the amino acid composition derived from the nucleotide sequence and that determined by amino acid analysis [31]. The agreement is very good, the exception being tryptophan which was determined by the fluorometric method of Pajot [32]. The presence of a single tryptophan (Trp199) is of interest because it may serve as a reporter group in fluorometric studies as it is located in the presumed NAD binding domain.…”
mentioning
confidence: 79%
“…The method of Pajot [38] was used for the determination of tryptophan. This method is based on a fluorescence intensity scale calibrated using standard solutions of N-acetyl-L-tryptophan amide and a correlation coefficient between the fluorescence of protein tryptophanyl residues and free tryptophan in the uniform environment provided by 7 M guanidine hydrochloride.…”
Section: Resultsmentioning
confidence: 99%
“…The concentration of the pure holoenzyme was determined spectrophotometrically using an extinction coefficient A2,*,,,,, = 1.65 cm2/mg or Awn,,, = 0.235 cm2/mg, estimated from quantitative tryptophan analysis (Pajot, 1976). For the apoenzyme, the extinction coefficient, A278nm = 1.07 cm2/mg, was calculated from the amino acid composition (Wetlaufer, 1962).…”
Section: Determination Of Protein Concentrationmentioning
confidence: 99%