Glycosides are a major group of plant secondary compounds characterized by one or more sugars conjugated to a lipophilic, possibly toxic aglycone, which is released upon hydrolysis. We compared small intestinal homogenate hydrolysis activity of three rodent and two avian species against four substrates: amygdalin and sinigrin, two plant-derived glucosides, the sugar lactose, whose hydrolysis mo...

The lipid moiety of a lipid diphosphate N-acetylglucosamine, an intermediate in glycosylation of proteins, was studied. Ozonolysis of the compound gave evidence for an alpha-saturated isoprene unit. Alkaline hydrolysis of the glycolipid, followed by high-pressure liquid chromatography, showed the presence of a series of polyprenol homologues identical with those isolated directly from Saccharom...

Uridine 2',3'-cyclic phosphonate (I) is slowly hydrolyzed by ribonuclease-A with k(2) and K(m) values at pH6 that are respectively 1900 and 15 times smaller than the same parameters at the same pH for the related phosphate (II). Since the ratio of rate constants for hydroxide ion catalyzed hydrolysis is about 4, this result is consistent with, but does not prove a mechanism for the enzymic reac...

The specificity of alkaline mesentericopeptidase (a proteinase closely related to subtilisin BPN') for the C-terminal moiety of the peptide substrate (Pi' specificity) has been studied in both hydrolysis and aminolysis reactions. N-Anthraniloylated peptide p-nitroanilides as fluorogenic substrates and amino acid or peptide derivatives as nucleophiles were used in the enzymic peptide hydrolysis ...

An intestinal perfusion technique has been used in normal human subjects to investigate the influence that starter protein composition and hydrolysis procedure have on absorption of amino acid residues from partial enzymic hydrolysates of whole protein. Five starter proteins were studied. Three (egg albumin, casein/soy/lactalbumin, and lactalbumin) were hydrolysed by papain, a second lactalbumi...

An intestinal perfusion technique has been used in normal human subjects to investigate the influence that starter protein composition and hydrolysis procedure have on absorption of amino acid residues from partial enzymic hydrolysates of whole protein. Five starter proteins were studied. Three (egg albumin, casein/soy/lactalbumin, and lactalbumin) were hydrolysed by papain, a second lactalbumi...

This reaction is catalyzed by Fragment A (mol wt 24,000) or other less common fragments generated by limited proteolysis and reduction of the toxin, but not by the toxin itself (mol wt 63,000). This report describes studies of the interaction of NAD+ with Fragment A. In addition to its major enzymic activity, Fragment A also catalyzes the slow hydrolysis of the nicotinamide-ribose linkage of NAD+.