2007
DOI: 10.1016/j.ijbiomac.2006.12.007
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A role of glycosyl moieties in the stabilization of bitter gourd (Momordica charantia) peroxidase

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Cited by 34 publications
(17 citation statements)
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“…This value was slightly higher than those reported for peroxidases from other sources, such as palm tree (51 and 57 kDa) (Sakharov, 2004), bitter gourd (43 kDa) (Fatima & Husain, 2007), sweet potato (37 kDa) (Castillo Leon et al, 2002), peanut (37-40 kDa) (van Huystee, Sun, & Lige, 2002), and wheat seedlings (23 kDa) (Lai et al, 2006). Most of the peroxidases reported to date are monomers.…”
Section: Molecular Massmentioning
confidence: 63%
See 1 more Smart Citation
“…This value was slightly higher than those reported for peroxidases from other sources, such as palm tree (51 and 57 kDa) (Sakharov, 2004), bitter gourd (43 kDa) (Fatima & Husain, 2007), sweet potato (37 kDa) (Castillo Leon et al, 2002), peanut (37-40 kDa) (van Huystee, Sun, & Lige, 2002), and wheat seedlings (23 kDa) (Lai et al, 2006). Most of the peroxidases reported to date are monomers.…”
Section: Molecular Massmentioning
confidence: 63%
“…The purified enzyme was more heat-stable than those reported peroxidases from other sources, such as strawberry (Civello et al, 1995), cotton (Triplett & Mellon, 1992), and horseradish roots (Moreno, Vázquez-Duhalt, & Nolasco, 1990). It has been shown that the thermal stability of peroxidase is due to the presence of a large number of cysteine residues in the polypeptide chain or glycosylation of the enzyme protein (Fatima & Husain, 2007;Triplett & Mellon, 1992).…”
Section: Optimum Ph Optimum Temperature and Thermal Stabilitymentioning
confidence: 83%
“…To study the positions of the tryptophan residues in the absence and presence of cosolvent, we have taken the ratio of relative fluorescence intensities at 320 and 360 nm as a probe [42], results are shown in Fig. 7B.…”
Section: Tryptophan Residues Get Buried At Low and Exposed At High Comentioning
confidence: 99%
“…Fig. 4B shows the changes in the ratio of RFI at 306 nm/350 nm as excited at 280 nm against increasing concentrations of alcohols, as a probe for global changes in the unfolded protein in the presence of various alcohols [38]. The change in conformation of the protein in the presence of increasing concentrations of methanol, ethanol and IP were insignificant.…”
Section: Alcohols Have Stabilized Tertiary Structure In U B State Of Bsamentioning
confidence: 99%