The enzyme capable to cleave trypsin active site titrant as substrate is a carboxylesterase with electrophoretic mobility similar to albumin.

J. Tözsér, T. M. Marsalkó, M. Punyiczki, P. Elödi

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

An enzyme isolated from Ehrlich ascites plasma and capable of cleaving trypsin active site titrant 4-nitrophenyl-p-guanidinobenzoate (Steven, F.S. and Al-Achmad, R.K. (1983) has been further investigated. The substrate hydrolysis follows Michaelis-Menten kinetics. The molecular mass of the enzyme is 50-70 kDa by gel filtration and SDS polyacrylamide gel electrophoresis. It has the mobility of albumin and coelutes with a carboxylesterase activity on a cation exchange column. (Cbz-Arg-NH)2-Rhodamine, the specific noncompetitive inhibitor of guanidinobenzoatase, also inhibits the carboxylesterase activity. Therefore, the guanidinobenzoatase activity of Ehrlich ascites plasma is a carboxylesterase (EC 3.1.1.1.) which likely originates from blood.

Original languageEnglish
Pages (from-to)57-65
Number of pages9
JournalActa biochimica et biophysica Hungarica
Volume25
Issue number1-2
Publication statusPublished - 1990

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry

Fingerprint Dive into the research topics of 'The enzyme capable to cleave trypsin active site titrant as substrate is a carboxylesterase with electrophoretic mobility similar to albumin.'. Together they form a unique fingerprint.

  • Cite this