acid-phosphatase and beta-naphthyl-phosphate

acid-phosphatase has been researched along with beta-naphthyl-phosphate* in 1 studies

Other Studies

1 other study(ies) available for acid-phosphatase and beta-naphthyl-phosphate

Article	Year
Bovine kidney low molecular weight acid phosphatase: FMN-dependent kinetics. Biochemistry and molecular biology international, 1997, Volume: 41, Issue:6 A low molecular weight bovine kidney acid phosphatase, electrophoretically homogeneous and with a relative molecular mass of 17.8 kDa, was used in this work. Among the various substrates tested, FMN was found to be the most effective, at pH 7.0. Distinct activation energy values were obtained for p-nitrophenyl phosphate- (45.44 kJ mol-1) and flavin mononucleotide- (28.60 kJ mol-1) hydrolysis reactions. The FMN hydrolysis was strongly inhibited by Cu2 and pCMB, but activated by guanosine. Pyridoxal-phosphate and vanadate were competitive inhibitors for the FMN-dependent reaction. Topics: Acid Phosphatase; Animals; Cattle; Chloromercuribenzoates; Copper; Electrophoresis, Polyacrylamide Gel; Flavin Mononucleotide; Guanosine; Hydrogen-Ion Concentration; Hydrolysis; Indicators and Reagents; Kidney; Kinetics; Molecular Weight; Naphthalenes; Nitrophenols; Organophosphates; Organophosphorus Compounds; p-Chloromercuribenzoic Acid; Phosphotyrosine; Pyridoxal Phosphate; Substrate Specificity; Vanadates	1997

Article

Year

Bovine kidney low molecular weight acid phosphatase: FMN-dependent kinetics.

Biochemistry and molecular biology international, 1997, Volume: 41, Issue:6

A low molecular weight bovine kidney acid phosphatase, electrophoretically homogeneous and with a relative molecular mass of 17.8 kDa, was used in this work. Among the various substrates tested, FMN was found to be the most effective, at pH 7.0. Distinct activation energy values were obtained for p-nitrophenyl phosphate- (45.44 kJ mol-1) and flavin mononucleotide- (28.60 kJ mol-1) hydrolysis reactions. The FMN hydrolysis was strongly inhibited by Cu2 and pCMB, but activated by guanosine. Pyridoxal-phosphate and vanadate were competitive inhibitors for the FMN-dependent reaction.

Topics: Acid Phosphatase; Animals; Cattle; Chloromercuribenzoates; Copper; Electrophoresis, Polyacrylamide Gel; Flavin Mononucleotide; Guanosine; Hydrogen-Ion Concentration; Hydrolysis; Indicators and Reagents; Kidney; Kinetics; Molecular Weight; Naphthalenes; Nitrophenols; Organophosphates; Organophosphorus Compounds; p-Chloromercuribenzoic Acid; Phosphotyrosine; Pyridoxal Phosphate; Substrate Specificity; Vanadates

1997