title: The enzyme capable to cleave trypsin active site titrant as substrate is a carboxylesterase with electrophoretic mobility similar to albumin.
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.
authors: Department of Biochemistry, Medical University of Debrecen, Hungary.
authors: J
authors: J
authors: Tözsér
authors: T M
authors: TM
authors: Marsalkó
authors: M
authors: M
authors: Punyiczki
authors: P
authors: P
authors: Elödi
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001565:Benzoates / Q000378:metabolism*; D002265:Carboxylic Ester Hydrolases / Q000097:blood / Q000737:chemistry / Q000378:metabolism*; D002286:Carcinoma, Ehrlich Tumor / Q000201:enzymology*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases; D006868:Hydrolysis; D007700:Kinetics; D051379:Mice; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012709:Serum Albumin / Q000737:chemistry*; D014357:Trypsin / Q000378:metabolism*
chemical_list: D001565:Benzoates; D012709:Serum Albumin; C002238:4-nitrophenyl 4'-guanidinobenzoate; D002265:Carboxylic Ester Hydrolases; C037288:guanidinobenzoate esterase; D010450:Endopeptidases; D014357:Trypsin