Isolation and study of a liver alpha-amylase. Comparison with glycogen phosphorylase activity.
An oligomaltosaccharide-forming amylase has been observed in mice liver crude homogenate. This enzyme has been isolated by binding to amylose. Some of its functional parameters have been studied and compared with those of glycogen phosphorylase demonstrating that amylase activity is not due to a glycogen phosphorylase isoenzyme. It has been further observed that amylase needs Ca2+ of Mg+2 and Cl- for its activity.
D000681:Amylases / Q000302:isolation & purification*; D000818:Animals; D002118:Calcium / Q000494:pharmacology; D004492:Edetic Acid / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D019811:Hydroxylamine; D006898:Hydroxylamines / Q000494:pharmacology; D008099:Liver / Q000201:enzymology*; D008274:Magnesium / Q000494:pharmacology; D051379:Mice; D006005:Phosphorylases / Q000378:metabolism*; D013696:Temperature; D000516:alpha-Amylases / Q000302:isolation & purification* / Q000378:metabolism
D006898:Hydroxylamines; D019811:Hydroxylamine; D004492:Edetic Acid; D006005:Phosphorylases; D000681:Amylases; D000516:alpha-Amylases; D008274:Magnesium; D002118:Calcium