[Proteolytic susceptibility of alpha-amylase of the pancreas of swine deprived of its structural calcium].
Hog pancreas alpha-amylase (alpha-1-4-glucan-glucan hydrolase, E.C. 3.2.1.1) lost its structural calcium by action of EDTA at 20 degrees C. Enzymatic activity experimented a decrease whereas a big increase in proteolytic susceptibility to bovine pancreas trypsin (E.C. 3.4.4.4) was shown. Native alpha-amylase had an activity of 2,730 mg maltose/min X mg enzyme and a Km of 0.222% amylose, the activity of calcium depleted amylase being of 1,640 mg maltose/min X mg enzyme and Km 0.571% amylose. Simple methods for evaluating proteolytic susceptibility of alpha-amylase micro-amounts against trypsin action, and for the measurement of alpha-amylase activity in polyacrylamide rod gels were also described.
D000818:Animals; D001051:Apoenzymes / Q000378:metabolism*; D001059:Apoproteins / Q000378:metabolism*; D002118:Calcium / Q000378:metabolism*; D004492:Edetic Acid / Q000008:administration & dosage; D006868:Hydrolysis; D007700:Kinetics; D010179:Pancreas / Q000201:enzymology*; D013552:Swine; D000516:alpha-Amylases / Q000378:metabolism*
D001051:Apoenzymes; D001059:Apoproteins; D004492:Edetic Acid; D000516:alpha-Amylases; D002118:Calcium
Susceptibilidad proteolítica de la alpha-amilasa de páncreas de cerdo privada de su calcio estructural.