Lysosomal peptidase measurement by sensitive fluorometric amino acid analysis

Stephen L Taylor, A. L. Tappel

Research output: Contribution to journalArticle

43 Citations (Scopus)

Abstract

A procedure has been developed for the measurement of lysosmal peptidase activity that is based upon highly sensitive fluorometric amino acid analysis. The fluorochrome results from the reaction of phthalaldehyde and mercaptoethanol with amino acids or similar compounds at pH 9.5. The fluorometric method is 10-100 times more sensitive than the colorimetric ninhydrin procedure for the measurement of lysosomal peptidases. The method lends itself to the measurement of any peptidase or protease that yields free amino groups in the product. The method has been applied to the measurement of cathepsin A and lysosomal dipeptidase activity.

Original languageEnglish (US)
Pages (from-to)140-148
Number of pages9
JournalAnalytical Biochemistry
Volume56
Issue number1
DOIs
StatePublished - Jan 1 1973

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Peptide Hydrolases
Amino Acids
Cathepsin A
Ninhydrin
Mercaptoethanol
Fluorescent Dyes

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Lysosomal peptidase measurement by sensitive fluorometric amino acid analysis. / Taylor, Stephen L; Tappel, A. L.

In: Analytical Biochemistry, Vol. 56, No. 1, 01.01.1973, p. 140-148.

Research output: Contribution to journalArticle

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