Abstract
α-Amylases of hog pancreas, human saliva and rat parotis are specifically precipitated from crude extracts as a glycogen-enzyme complex insoluble in 40% ethanol. The specific activity (units/mg protein) of the enzymes thus precipitated approaches or is equal to that of the best crystalleine prepations. The procedure is readily carried out on a micro-scale. A method for the removal of glycogen from the complex, with the subsequent preparation of the crystalline pancreatic and parotis enzymes, is described. In the case of pancreatic amylase the enzyme-glycogen complex contains one mole of enzyme per 550 anhydroglucose units.
| Original language | English |
|---|---|
| Pages (from-to) | 200-206 |
| Number of pages | 7 |
| Journal | Biochimica et Biophysica Acta - General Subjects |
| Volume | 65 |
| Issue number | 2 |
| DOIs | |
| State | Published - 4 Dec 1962 |
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