A phage antibody to the active site of human placental alkaline phosphatase with higher affinity to the enzyme–substrate complex

Jain, Vishal; Saini, Deepika; Goswami, Pooja; Sinha, Subrata

doi:10.1016/j.molimm.2006.02.024

Cited by 2 publications

(1 citation statement)

References 29 publications

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“…After removal of debris, the supernatant was subjected to affinity chromatography as outlined earlier (Koebsch et al, 2009). Fractions were tested for phosphatase activity against the substrate pNPP (p-nitrophenyl-phosphate), and the released p-nitrophenol (405 nm) was quantified by use of a photometer (Jain et al, 2007).…”

Section: Isolation Of the Fusion Protein And Test For Enzymatic Activitymentioning

confidence: 99%

AStreptomyces-specific member of the metallophosphatase superfamily contributes to spore dormancy and interaction withAspergillus proliferans

Lamp

Weber

Cingöz

et al. 2013

FEMS Microbiol Lett

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We have identified, cloned and characterized a formerly unknown protein from Streptomyces lividans spores. The deduced protein belongs to a novel member of the metallophosphatase superfamily and contains a phosphatase domain and predicted binding sites for divalent ions. Very close relatives are encoded in the genomic DNA of many different Streptomyces species. As the deduced related homologues diverge from other known phosphatase types, we named the protein MptS (metallophosphatase type from Streptomyces). Comparative physiological and biochemical investigations and analyses by fluorescence microscopy of the progenitor strain, designed mutants carrying either a disruption of the mptS gene or the reintroduced gene as fusion with histidine codons or the egfp gene led to the following results: (i) the mptS gene is transcribed in the course of aerial mycelia formation. (ii) The MptS protein is produced during the late stages of growth, (iii) accumulates within spores, (iv) functions as an active enzyme that releases inorganic phosphate from an artificial model substrate, (v) is required for spore dormancy and (vi) MptS supports the interaction amongst Streptomyces lividans spores with conidia of the fungus Aspergillus proliferans. We discuss the possible role(s) of MptS-dependent enzymatic activity and the implications for spore biology.

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Section: Isolation Of the Fusion Protein And Test For Enzymatic Activitymentioning

confidence: 99%

AStreptomyces-specific member of the metallophosphatase superfamily contributes to spore dormancy and interaction withAspergillus proliferans

Lamp

Weber

Cingöz

et al. 2013

FEMS Microbiol Lett

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show abstract

Humanization of high affinity anti-HBs antibody by using human consensus sequence and modification of selected minimal positional template and packing residues

Tiwari

Khanna

Acharya

et al. 2009

Vaccine

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A phage antibody to the active site of human placental alkaline phosphatase with higher affinity to the enzyme–substrate complex

Cited by 2 publications

References 29 publications

AStreptomyces-specific member of the metallophosphatase superfamily contributes to spore dormancy and interaction withAspergillus proliferans

AStreptomyces-specific member of the metallophosphatase superfamily contributes to spore dormancy and interaction withAspergillus proliferans

Humanization of high affinity anti-HBs antibody by using human consensus sequence and modification of selected minimal positional template and packing residues

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