Approaches to the mechanism of action of double-headed enzymes.
Explore the source record for details and available documents.
Biomedical subjects
Publications and source records attributed to E RACKER.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Acetyl phosphate and 1,3-diphosphoglycerate react with glyceraldehyde-3-phosphate dehydrogenase to form relatively stable enzyme substrate compounds. These compounds appear to be thiol esters, and their properties indicate that they are intermediates in the catalytic activity of the enzyme: they undergo hydrolysis and arsenolysis in the presence of DPN and are reduced by DPNH to form aldehydes. These results are in agreement with the mechanism previously proposed for the oxidation of aldehydes in which a thiol ester formed on the enzyme, with concomitant reduction of DPN, is split in the presence of phosphate to acyl phosphate and regenerated enzyme.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
A mucopolysaccharide has been obtained from intestinal tissue of adult mice which inhibits both infectivity and hemagglutination of Theiler's GDVII strain of encephalomyelitis virus of mice. The inhibitor is inactive against the FA and TO strains of Theiler's virus and against the Lansing strain of poliomyelitis virus. In the adult mouse, large amounts of the inhibitor are found only in the small intestine. The small intestine of infant mice, however, contains a considerably smaller amount of inhibitor. Inhibition, both in vivo and in vitro, appears to be the result of an interaction between virus and inhibitor. The intestines of man, monkey, rabbit, rat, cotton rat, hamster, sheep, cow, and pig contain relatively little inhibitor whereas guinea pig intestine contains as much as adult mouse intestine. An enzyme was found in the feces of mice, and several other animals, which is capable of destroying the inhibitory activity of the mucopolysaccharide with the liberation of reducing sugars.