Transamidating enzymes. II. A continuous fluorescent method suited for automating measurements of factor XIII in plasma

L. Lorand, O. M. Lockridge, L. K. Campbell, R. Myhrman, J. Bruner-Lorand

Research output: Contribution to journalArticle

85 Scopus citations

Abstract

The covalent incorporation of monodansylcadaverine (N-5-(aminopentyl)-5-dimethylamino-1-naphthalenesulfonamide) into some proteins, catalyzed by a variety of transamidases, is accompanied by marked changes in the fluorescence emission of the dansyl group. In addition to a blue shift, there is an increase in intensity of fluorescence. Various types of caseins, as well as succinylated β-lactoglobulin or lysozyme, can be used as protein acceptors, though neither of the latter two support the reaction in their native form. The continuous rise of fluorescence intensity made it possible to record directly the course of the enzymic transamidating reactions. As such, the procedure is well suited for automation. Furthermore, the assay is applicable to human plasma for the monitoring of fibrin-stabilizing factor (Factor XIII) levels.

Original languageEnglish (US)
Pages (from-to)221-231
Number of pages11
JournalAnalytical Biochemistry
Volume44
Issue number1
DOIs
StatePublished - Nov 1971

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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