2014
DOI: 10.1016/j.phytochem.2014.02.010
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Purification and characterization of tyrosinase from walnut leaves (Juglans regia)

Abstract: Graphical abstractTyrosinase from walnut leaves (Juglans regia) corresponding to the known jrPPO1 sequence was purified and characterized. Two major tyrosinase forms differing only in their C-termini were identified. The first form (jrPPO1(Asp101 → Pro444)) is one amino acid shorter than the second form (jrPPO1(Asp101 → Arg445)).

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Cited by 78 publications
(86 citation statements)
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“…By applying the method described by Zekiri et al (2014), the enzyme was purified to homogeneity. Initial attempts to crystallize the most abundant form jrPPO1(Asp 101 -Arg 445 ), as described in Zekiri et al (2014), covering a wide range of crystallization conditions proved to be very successful.…”
Section: Resultsmentioning
confidence: 99%
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“…By applying the method described by Zekiri et al (2014), the enzyme was purified to homogeneity. Initial attempts to crystallize the most abundant form jrPPO1(Asp 101 -Arg 445 ), as described in Zekiri et al (2014), covering a wide range of crystallization conditions proved to be very successful.…”
Section: Resultsmentioning
confidence: 99%
“…Initial attempts to crystallize the most abundant form jrPPO1(Asp 101 -Arg 445 ), as described in Zekiri et al (2014), covering a wide range of crystallization conditions proved to be very successful. Crystals suitable for X-ray diffraction experiments were obtained using 30% PEG 5000 MME, 200 mM ammonium sulfate, 100 mM MES pH 6.5 (Fig.…”
Section: Resultsmentioning
confidence: 99%
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“…In connection with the discovery of the JrPPO genes, a tyrosinase was isolated from J. regia leaves and identified as a PPO corresponding to the known JrPPO1 sequence (Zekiri et al 2014). Tyrosinases can catalyze both ortho-hydroxylation of monophenols to odiphenols (monophenolase activity) and the subsequent oxidation of o-diphenols to the corresponding o-quinones (diphenolase activity).…”
Section: Proteomics Researchmentioning
confidence: 99%