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

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

Research output: Contribution to journalArticle

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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

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Electrophoretic mobility
Carboxylesterase
Trypsin
Albumins
Catalytic Domain
Ascites
Substrates
Enzymes
Plasmas
Rhodamines
Molecular mass
Electrophoresis
Gel Chromatography
Cations
Polyacrylamide Gel Electrophoresis
Hydrolysis
Blood
Gels
Kinetics
guanidinobenzoate esterase

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics

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The enzyme capable to cleave trypsin active site titrant as substrate is a carboxylesterase with electrophoretic mobility similar to albumin. / Tőzsér, J.; Marsalkó, T. M.; Punyiczki, M.; Elödi, P.

In: Acta Biochimica et Biophysica Hungarica, Vol. 25, No. 1-2, 1990, p. 57-65.

Research output: Contribution to journalArticle

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