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- W2007156778 abstract "A fourth molecular form of α-galactosidase has been discovered in leaves of Cucurbita pepo and a 6-fold purification achieved by ammonium sulphate precipitation and ion exchange chromatography. The enzyme designated LIV has the unique property among α-galactosidases of possessing an alkaline pH optimum at 7.5 with p-nitrophenyl-α-D-galactopyranoside (PNPG) or stachyose as substrates. Raffinose hydrolysis was optimal at pH 6.5–7.0. A Km-value of 0.60 mM for PNPG hydrolysis was obtained. In immature importing leaves LIV activity was about 3-fold higher than the total acid α-galactosidase activity. Through the transition phase, during which the leaf changes from an importing to an exporting organ, a 6-fold decline in LIV activity occured. In mature leaves LIV activity was about 60% of the total acid α-galactosidase activity. It is suggested that LIV may play a major role in the hydrolysis of stachyose imported into immature leaves." @default.
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- W2007156778 title "Alkaline α-galactosidase in leaves of Cucurbita pepo" @default.
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- W2007156778 doi "https://doi.org/10.1016/0304-4211(82)90023-2" @default.
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