TY - JOUR
T1 - The glycogen-amylase complex as a means of obtaining highly purified α-amylases
AU - Loyter, Abraham
AU - Schramm, Michael
PY - 1962/12/4
Y1 - 1962/12/4
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0001757520&partnerID=8YFLogxK
U2 - 10.1016/0006-3002(62)91039-9
DO - 10.1016/0006-3002(62)91039-9
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C2 - 13931324
AN - SCOPUS:0001757520
SN - 0006-3002
VL - 65
SP - 200
EP - 206
JO - Biochimica et Biophysica Acta - General Subjects
JF - Biochimica et Biophysica Acta - General Subjects
IS - 2
ER -