A novel 35 kDa frog liver acid metallophosphatase
The lower molecular weight (35 kDa) acid phosphatase from the frog ( Rana esculenta) liver is a glycometalloenzyme susceptible to activation by reducing agents and displaying tartrate and fluoride resistance. Metal chelators (EDTA, 1,10-phenanthroline) inactivate the enzyme reversibly in a time- and...
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Published in | Biochimica et biophysica acta Vol. 1431; no. 1; pp. 199 - 211 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
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Netherlands
Elsevier B.V
12.04.1999
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Abstract | The lower molecular weight (35 kDa) acid phosphatase from the frog (
Rana esculenta) liver is a glycometalloenzyme susceptible to activation by reducing agents and displaying tartrate and fluoride resistance. Metal chelators (EDTA, 1,10-phenanthroline) inactivate the enzyme reversibly in a time- and temperature-dependent manner. The apoenzyme is reactivated by divalent transition metal cations, i.e. cobalt, zinc, ferrous, manganese, cadmium and nickel to 130%, 75%, 63%, 62%, 55% and 34% of the original activity, respectively. Magnesium, calcium, cupric and ferric ions were shown to be ineffective in this process. Metal analysis by the emission spectrometry method (inductively coupled plasma-atomic emission spectrometry) revealed the presence of zinc, iron and magnesium. The time course of the apoenzyme reactivation, the stabilization effect and the relatively high resistance to oxidizing conditions indicate that the zinc ion is crucial for the enzyme activity. The presence of iron was additionally confirmed by the visible absorption spectrum of the enzyme with a shoulder at 417 nm and by the electron paramagnetic resonance line of high spin iron(III) with
g
eff of 2.4. The active center containing only zinc or both zinc and iron ions is proposed. The frog liver lower molecular weight acid phosphatase is a novel metallophosphatase of lower vertebrate origin, distinct from the mammalian tartrate-resistant, purple acid phosphatases. |
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AbstractList | The lower molecular weight (35 kDa) acid phosphatase from the frog (Rana esculenta) liver is a glycometalloenzyme susceptible to activation by reducing agents and displaying tartrate and fluoride resistance. Metal chelators (EDTA, 1,10-phenanthroline) inactivate the enzyme reversibly in a time- and temperature-dependent manner. The apoenzyme is reactivated by divalent transition metal cations, i. e. cobalt, zinc, ferrous, manganese, cadmium and nickel to 130%, 75%, 63%, 62%, 55% and 34% of the original activity, respectively. Magnesium, calcium, cupric and ferric ions were shown to be ineffective in this process. Metal analysis by the emission spectrometry method (inductively coupled plasma-atomic emission spectrometry) revealed the presence of zinc, iron and magnesium. The time course of the apoenzyme reactivation, the stabilization effect and the relatively high resistance to oxidizing conditions indicate that the zinc ion is crucial for the enzyme activity. The presence of iron was additionally confirmed by the visible absorption spectrum of the enzyme with a shoulder at 417 nm and by the electron paramagnetic resonance line of high spin iron(III) with geff of 2.4. The active center containing only zinc or both zinc and iron ions is proposed. The frog liver lower molecular weight acid phosphatase is a novel metallophosphatase of lower vertebrate origin, distinct from the mammalian tartrate-resistant, purple acid phosphatases. The lower molecular weight (35 kDa) acid phosphatase from the frog ( Rana esculenta) liver is a glycometalloenzyme susceptible to activation by reducing agents and displaying tartrate and fluoride resistance. Metal chelators (EDTA, 1,10-phenanthroline) inactivate the enzyme reversibly in a time- and temperature-dependent manner. The apoenzyme is reactivated by divalent transition metal cations, i.e. cobalt, zinc, ferrous, manganese, cadmium and nickel to 130%, 75%, 63%, 62%, 55% and 34% of the original activity, respectively. Magnesium, calcium, cupric and ferric ions were shown to be ineffective in this process. Metal analysis by the emission spectrometry method (inductively coupled plasma-atomic emission spectrometry) revealed the presence of zinc, iron and magnesium. The time course of the apoenzyme reactivation, the stabilization effect and the relatively high resistance to oxidizing conditions indicate that the zinc ion is crucial for the enzyme activity. The presence of iron was additionally confirmed by the visible absorption spectrum of the enzyme with a shoulder at 417 nm and by the electron paramagnetic resonance line of high spin iron(III) with g eff of 2.4. The active center containing only zinc or both zinc and iron ions is proposed. The frog liver lower molecular weight acid phosphatase is a novel metallophosphatase of lower vertebrate origin, distinct from the mammalian tartrate-resistant, purple acid phosphatases. |
Author | Szalewicz, Agata Radomska, Barbara Strzelczyk, Barbara Kubicz, Aleksandra |
Author_xml | – sequence: 1 givenname: Agata surname: Szalewicz fullname: Szalewicz, Agata email: agata@bf.uni.wroc.pl organization: Institute of Biochemistry and Molecular Biology, University of Wrocław, Tamka 2, 50-137 Wrocław, Poland – sequence: 2 givenname: Barbara surname: Radomska fullname: Radomska, Barbara organization: Department of Chemistry, University of Wrocław, Joliot-Curie 14, 50-383 Wrocław, Poland – sequence: 3 givenname: Barbara surname: Strzelczyk fullname: Strzelczyk, Barbara organization: Institute of Biochemistry and Molecular Biology, University of Wrocław, Tamka 2, 50-137 Wrocław, Poland – sequence: 4 givenname: Aleksandra surname: Kubicz fullname: Kubicz, Aleksandra organization: Institute of Biochemistry and Molecular Biology, University of Wrocław, Tamka 2, 50-137 Wrocław, Poland |
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Keywords | BSA, bovine serum albumin pNPP, p-nitrophenyl phosphate BCA, bicinchoninic acid Metalloenzyme HMW AcPase, high molecular weight acid phosphatase LMW AcPase, lower molecular weight acid phosphatase OP, 1,10-phenanthroline ( o-phenanthroline) DTT, dithiothreitol PAP, purple acid phosphatase PMSF, phenylmethylsulfonyl fluoride Con A, concanavalin A EDTA, ethylenediaminetetraacetate disodium salt Metallophosphatase Divalent metal cation Frog liver Acid phosphatase AcPase, acid phosphatase TRAP, tartrate-resistant acid phosphatase |
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Snippet | The lower molecular weight (35 kDa) acid phosphatase from the frog (
Rana esculenta) liver is a glycometalloenzyme susceptible to activation by reducing agents... The lower molecular weight (35 kDa) acid phosphatase from the frog (Rana esculenta) liver is a glycometalloenzyme susceptible to activation by reducing agents... |
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SubjectTerms | Acid phosphatase Acid Phosphatase - chemistry Animals Apoenzymes - chemistry Cations - pharmacology Chelating Agents - pharmacology Divalent metal cation Electron Spin Resonance Spectroscopy Enzyme Activation Enzyme Reactivators Enzyme Stability Frog liver Liver - enzymology Metalloenzyme Metallophosphatase Metals - analysis Metals - pharmacology Molecular Weight Rana esculenta |
Title | A novel 35 kDa frog liver acid metallophosphatase |
URI | https://dx.doi.org/10.1016/S0167-4838(99)00029-1 https://www.ncbi.nlm.nih.gov/pubmed/10209292 https://search.proquest.com/docview/69700462 |
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