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P9041

Sigma-Aldrich

Phosphodiesterase II from bovine spleen

lyophilized powder, ≥5.0 units/mg protein

Synonyme(s) :

3′-Exonuclease, Spleen exonuclease, Spleen phosphodiesterase

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172,00 €
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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

172,00 €


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Forme

lyophilized powder

Activité spécifique

≥5.0 units/mg protein

Poids mol.

65 kDa

Numéro d'accès UniProt

Activité étrangère

5′-Nucleotidase ≤1% of base activity

Température de stockage

−20°C

Informations sur le gène

Description générale

Research area: Cell signaling. Phosphodiesterase (PDE) II belongs to the PDE superfamily and includes subtypes from one to 11.[1] They exist as a dimer and comprise of N-terminal regulatory domain, C-terminal prenylated domain, and a Zn2+containing catalytic domain.[1] The bovine spleen PDE2 corresponds to a molecular weight of 65 kDa. It requires divalent cations for its enzymatic activity and has an optimum pH of 7.5.[2]

Application

Phosphodiesterase (PDE) is any enzyme that is used to break phosphodiester bonds. It is a membrane-bound glycoprotein that is used to catalyze the hydrolysis of various nucleotide polyphosphates. Phosphodiesterase II has been used in the enzymatic digestions of purified proteins such as the P8-dGMP complex[3]. Bovine spleen phosphodiesterase has been used to digest N-cadherin[4]. Phosphodiesterase II from bovine is suitable for sequential and end-group analysis of poly and oligonucleotides. It may be used in kinetic studieson substrate degradation of macro-molecules.
Phosphodiesterase II from bovine spleen has been used in the:
  • excision of pyridyloxobutyl (POB) base adducts from DNA[5]
  • digestion of DNA prior to cycloadenosine enrichment[6]
  • hydrolysis of DNA from blue mussels gill tissue into deoxyribonucleoside 3′-monophosphates[7]

The product has been used in the characterization of polynucleotide chain length, base composition, and identity of terminal nucleotide. The enzyme has also been used in excision of pyridyloxobutyl (POB) base adducts from DNA.[5] Furthermore, it has been used along with micrococcal endonuclease to hydrolyze purified DNA to 3 -nucleoside monophosphates.[8]

Actions biochimiques/physiologiques

Hydrolyzes RNA, RNA-Core, 3′-alkyl- and 3′-aryl-nucleoside phosphates, and polydeoxyribonucleotides with 3′-phosphate end groups to 3′-mononucleotides.
Polynucleotides having 5′-phosphomonoester end groups are not attacked.
Phosphodiesterase (PDE) breaks phosphodiester bonds.[9] 3-Isobutyl-methylxanthine (IBMX) is a potential PDE2 inhibitor.[10]
The enzyme acts on poly(A), poly(U), and poly(I). Native DNA and poly(C) are quite resistant to the action of this enzyme.

Définition de l'unité

One unit will produce acid soluble nucleotides equivalent to a ΔA260 of 16 in 30 min at pH 6.5 at 37 °C, in a 2.0 mL reaction mixture. Substrate: RNA-Core. Actual A260 is measured on the supernatant after precipitation of the unhydrolyzed RNA with uranyl acetate-perchloric acid reagent.

Remarque sur l'analyse

Protein determined by biuret

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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Les clients ont également consulté

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Hong Feng et al.
Biochemistry, 44(34), 11486-11495 (2005-08-24)
Endonuclease V is an enzyme that initiates a conserved DNA repair pathway by making an endonucleolytic incision at the 3' side one nucleotide from a deaminated base lesion. Site-directed mutagenesis analysis was conducted at seven conserved motifs of the thermostable
Dynamic regulation of cAMP signaling by cGMP in the cardiovascular system: roles of phosphodiesterase 2 and phosphodiesterase 3 enzymes.
Donald H Maurice
Proceedings of the Western Pharmacology Society, 46, 32-36 (2004-01-01)
D H Bamford et al.
Journal of virology, 50(2), 309-315 (1984-05-01)
DNA of bacteriophage PRD1 has protein P8 at its termini. Extracts of infected cells are able to derivatize P8 in vitro with labeled dGTP. Two early proteins, P1 and P8, products of genes I and VIII, respectively, are the only
Halldora Skarphedinsdottir et al.
Mutation research, 702(1), 24-31 (2010-07-21)
Adult and young herring gulls (Larus argentatus) in Sweden and Iceland were investigated with respect to DNA adducts, analysed with the nuclease-P1 version of the (32)P-postlabelling method, and micronucleated erythrocytes. Three important aims were: (1) to estimate the degree of
Zh K Nazarkina et al.
Biochemistry. Biokhimiia, 70(12), 1327-1334 (2006-01-19)
To investigate interactions between proteins participating in the long-patch pathway of base excision repair (BER), DNA duplexes with flap strand containing modifications in sugar phosphate backbone within the flap-forming oligonucleotides were designed. When the flap-forming oligonucleotide consisted of two sequences

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