Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.20 (alpha-glucosidase)
 4,237 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In Echinodontium tinctorium the presence of the following enzymes was demonstrated: esterase, maltase, lactase, sucrase, raffinase, diastase, inulase, cellulase, hemicellulase, urease, rennet, and catalase.
J Gen Physiol 1920 Jul 20
PMID:ENZYME ACTION IN ECHINODONTIUM TINCTORIUM ELLIS AND EVERHART. 1987 34

Circumstantial evidence is presented which indicates that Polyporus volvatus is parasitic. Cultures of Polyporus volvatus and Fomes igniarius may be obtained from the young sporophores by the tissue method. In Polyporus volvatus the presence of the following enzymes was demonstrated: esterase, maltase, lactase, sucrase, raffinase, diastase, inulase, cellulase, hemicellulase, glucosidase, rennet, and catalase. In Fomes igniarius the presence of the following enzymes was demonstrated: esterase, maltase, lactase, sucrase, raffinase, diastase, inulase, cellulase, hemicellulase, glucosidase, urease, rennet, and catalase.
J Gen Physiol 1921 Jul 20
PMID:STUDIES IN WOOD DECAY : II. ENZYME ACTION IN POLYPORUS VOLVATUS PECK AND FOMES IGNIARIUS (L.) GILLET. 1987 5

1. Considering previously published data on the velocity of hydrolysis of glucosides by acids, it is shown that phloridzin, judged from the standpoint of the velocity coefficient and the critical increment for hydrolysis, resembles the gamma-fructosides (sucrose, raffinose and melezitose) more closely than it does the normal glucosides (salicin, arbutin, maltose, etc.). 2. Previous work on the enzymic hydrolysis of phloridzin shows that it is not hydrolysed by emulsin, but that it is hydrolysed by some other enzyme which occurs fairly freely in nature. 3. The difficulty in examining the enzymic hydrolysis of phloridzin lies in its very low solubility. It has been shown, in confirmation of earlier work, that emulsin is definitely without action on phloridzin at various values of pH and of temperature. This result is difficult to reconcile with the beta-glucosidic character commonly ascribed to phloridzin, and with the fact that emulsin hydrolyses (synthetic) phloroglucinol-beta-glucoside, of which phlorizin is regarded as a derivative. 4. Phloridzin is hydrolysed by a yeast maltase preparation, known to contain saccharase. Phloridzin is readily attacked by maltase-free saccharase at 30 degrees C. and pH of 4.45. If the alpha-glucase of the sucrose-splitting enzyme is (as stated) inactive under these conditions, then the enzyme responsible for the hydrolysis of phloridzin is beta-(gamma) fructosidase. 5. The sugar prepared from phloridzin differs from glucose in its specific rotation and in its action towards Bacillus pestis.
J Gen Physiol 1930 Jul 20
PMID:THE ENZYMIC HYDROLYSIS OF PHLORIDZIN. 1987 65

1. The pH-activity relationship of invertase has been studied in vivo and in vitro under identical external environmental conditions. 2. The effect of changing (H(+)) upon the sucroclastic activity of living cells of S. cerevisiae and of invertase solutions obtained therefrom has been found, within experimental error, to be identical. 3. The region of living yeast cells in which invertase exerts its physiological activity changes its pH freely and to the same extent as that of the suspending medium. It is suggested that this may indicate that this intracellular enzyme may perform its work somewhere in the outer region of the cell. 4. In using live cells containing maltase, no evidence of increased sucroclastic activity around pH 6.9, due to the action of Weidenhagen's alpha-glucosidase (maltase), was found.
J Gen Physiol 1932 Nov 20
PMID:SIMILARITY OF THE KINETICS OF INVERTASE ACTION IN VIVO AND IN VITRO. II. 1987 2

1. The maltase of saliva and that of E. coli (B. coli communis) hydrolyze maltose but not alpha-methylglucoside or sucrose and are therefore to be considered glucomaltases. 2. Maltase is rapidly and completely inactivated and digested by trypsin.
J Gen Physiol 1933 May 20
PMID:THE DIGESTION AND INACTIVATION OF MALTASE BY TRYPSIN AND THE SPECIFICITY OF MALTASES. 1987 37


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