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Studies on enzyme action. XI.-Hydrolysis of raffinose by acids and enzymes
Author(s) -
HENRY E. ARMSTRONG,
Walter Hamis Glover
Publication year - 1908
Publication title -
proceedings of the royal society of london series b containing papers of a biological character
Language(s) - English
Resource type - Journals
eISSN - 2053-9185
pISSN - 0950-1193
DOI - 10.1098/rspb.1908.0030
Subject(s) - salicin , raffinose , maltose , chemistry , hydrolysis , enzyme , sugar , melibiose , biochemistry , galactosidases , glucoside , sucrose , beta galactosidase , gene expression , gene , medicine , alternative medicine , pathology
In a previous communication of this series (vol. 74, p. 191), it is pointed out that the various glucosides are hydrolysed by acids at very different rates, the relative values being approximately of the order shown in the following table:-α -Methylglucoside....100β -Methylglucoside....180α -Methylglucoside....540β -Methylglucoside....880 Salicin (a β -glucoside)....600 Milk-sugar (α β -galactoside)....720 Maltose (anα -glucoside)....740 Cane-sugar, it is to be remembered, is hydrolysed at a rate vastly more rapid-at least 1000 times as rapidly as maltose, in fact. These differences, taking into account the peculiar specific behaviour of enzymes as hydrolytic agents, raise questions of interest from the chemical side and they are of no slight significance perhaps also from a biological point of view.

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