@entity69630 (EC 3.2.1.1) was purified from the muscle and intestine of the parasitic helminth of @entity1707 @entity10130 . The enzymes from the two sources differed in their properties. Isoelectric focusing revealed one form of a-amylase from muscles with pl of 5.0, and two forms of amylase from intestine with pI of 4.7 and 4.5. @entity214 /PAGE suggested a molecular mass of 83 kDa and 73 kDa for isoenzymes of a-amylases from intestine and 59 kDa for the muscle enzyme. @entity69630 from intestine showed maximum activity at pH 7.4, and the enzyme from muscle at pH 8.2. The muscle enzyme was more thermostabile than the intestinal @entity69630 . Both the muscle and intestine amylase lost half of its activity after 15 min at 70 degrees C and 50 degrees C, respectively. The Km values were: for muscle amylase 0.22 microg/ml glycogen and 3.33 microg/ml starch, and for intestine amylase 1.77 microg/ml glycogen and 0.48 microg/ml starch. Both amylases were activated by @entity141 and inhibited by @entity1098 , @entity13638 , @entity18041 and the inhibitor of a-amylase from @entity3505 . No significant differences were found between the properties of a-amylases from parasites and from their hosts.

Purification and characterization of alpha-amylases from the intestine and muscle of XXXX (Nematoda).

@entity1707 :: ('9823', 'Species') :: ['pigs'] @entity3505 :: ('4565', 'Species') :: ['wheat'] @entity13638 :: ('MESH:D019807', 'Chemical') :: ['iodoacetic acid'] @entity69630 :: ('100153854(Tax:9823)', 'Gene') :: ['alpha-amylase', 'Alpha-Amylase'] @entity18041 :: ('CHEBI:28420', 'Chemical') :: ['p-chloromercuribenzoate'] @entity141 :: ('CHEBI:29108', 'Chemical') :: ['Ca2+'] @entity10130 :: ('6253', 'Species') :: ['Ascaris suum'] @entity1098 :: ('MESH:D004492', 'Chemical') :: ['EDTA'] @entity214 :: ('CHEBI:8984', 'Chemical') :: ['SDS']
@entity10130 :: (6253,Species) :: ['ascaris suum']
