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Literature summary for 1.11.1.6 extracted from

  • Riccardi, C.M.; Cole, K.S.; Benson, K.R.; Ward, J.R.; Bassett, K.M.; Zhang, Y.; Zore, O.V.; Stromer, B.; Kasi, R.M.; Kumar, C.V.
    Toward "stable-on-the-table" enzymes improving key properties of catalase by covalent conjugation with poly(acrylic acid) (2014), Bioconjug. Chem., 25, 1501-1510 .
    View publication on PubMed

Application

Application Comment Organism
synthesis improvement of thermal stability, resistance to protease degradation, and resistance to ascorbate inhibition, while retaining enzyme structure and activity, by conjugation to poly(acrylic acid). 55-80% and 90-100% activity is retained for all samples synthesized at pH 5.0 and pH 7.0, respectively, Km or Vmax values do not differ significantly from those of the free enzyme. Conjugates synthesized at pH 7.0 are thermally stable up to 85-90°C, and retain 40-90% of their original activities after storing for 10 weeks at 8°C Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus P00432
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Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
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Bos taurus
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liver
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Bos taurus
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Synonyms

Synonyms Comment Organism
CAT
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Bos taurus