A2643
α-Amylase from porcine pancreas
Type VII-A, DFP treated, ammonium sulfate suspension, ≥500 units/mg protein (E1%/280)
Synonym(s):
β-N-acetylglucosaminidase porcine placenta, PPA, al1,4 glucan-4-glucanohydrolase,, porcine pancreas α-amylase
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About This Item
UNSPSC Code:
12352204
MDL number:
type
Type VII-A
form
ammonium sulfate suspension
specific activity
≥500 units/mg protein (E1%/280)
storage temp.
2-8°C
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General description
Molecular mass: 51-54 kDa.
α-Amylase isolated from porcine pancreas is a glycoprotein. It is a single polypeptide chain of ~475 residues containing two SH groups and four disulfide bridges and a tightly bound Ca2+ necessary for stability. Chloride ions are necessary for activity and stability. The pH range for activity is 5.5 to 8.0, with the pH optimum at 7.
α-Amylase isolated from porcine pancreas is a glycoprotein. It is a single polypeptide chain of ~475 residues containing two SH groups and four disulfide bridges and a tightly bound Ca2+ necessary for stability. Chloride ions are necessary for activity and stability. The pH range for activity is 5.5 to 8.0, with the pH optimum at 7.
Physical form
Suspension in 3.2 M (NH4)2SO4, pH 6.1
Other Notes
One unit will liberate 1.0 mg of maltose from starch in 3 min at pH 6.9 at 20 °C.
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
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Fushan Liu et al.
Journal of experimental botany, 60(15), 4423-4440 (2009-10-07)
The amylose extender (ae(-)) mutant of maize lacks starch branching enzyme IIb (SBEIIb) activity, resulting in amylopectin with reduced branch point frequency, and longer glucan chains. Recent studies indicate isozymes of soluble starch synthases form high molecular weight complexes with
Buford L Nichols et al.
The Journal of nutrition, 139(4), 684-690 (2009-02-06)
Starch is the major source of food glucose and its digestion requires small intestinal alpha-glucosidic activities provided by the 2 soluble amylases and 4 enzymes bound to the mucosal surface of enterocytes. Two of these mucosal activities are associated with
Phuong Lan Tran et al.
FEBS letters, 588(4), 620-624 (2014-01-21)
The action pattern of Bacillus licheniformis thermostable α-amylase (BLA) was analyzed using a series of (14)C-labeled and non-labeled maltooligosaccharides from maltose (G2) to maltododecaose (G12). Maltononaose (G9) was the preferred substrate, and yielded the smallest Km=0.36 mM, the highest kcat=12.86
Hongyu Wang et al.
Molecules (Basel, Switzerland), 18(2), 2255-2265 (2013-02-23)
Characterization of polyphenolic compounds in the stems of P. multiflorum was conducted using HPLC, high resolution LC-MS and LC-MSn. Proanthocyanidins in particular were isolated in 4.8% yield using solvent extraction followed by Sephadex LH-20 fractionation. HPLC analysis using a diol
Jean-Luc Da Lage et al.
BMC evolutionary biology, 13, 40-40 (2013-02-15)
Increasing genome data show that introns, a hallmark of eukaryotes, already existed at a high density in the last common ancestor of extant eukaryotes. However, intron content is highly variable among species. The tempo of intron gains and losses has
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