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
Sign Into View Organizational & Contract Pricing
All Photos(1)
About This Item
Pricing and availability is not currently available.
Recommended Products
type
Type VII-A
form
ammonium sulfate suspension
specific activity
≥500 units/mg protein (E1%/280)
storage temp.
2-8°C
Looking for similar products? Visit Product Comparison Guide
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.
Unit Definition
One unit will liberate 1.0 mg of maltose from starch in 3 min at pH 6.9 at 20 °C.
Physical form
Suspension in 3.2 M (NH4)2SO4, pH 6.1
Other Notes
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
comparable product
Product No.
Description
Pricing
inhibitor
Product No.
Description
Pricing
substrate
Choose from one of the most recent versions:
Certificates of Analysis (COA)
Lot/Batch Number
Don't see the Right Version?
If you require a particular version, you can look up a specific certificate by the Lot or Batch number.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Customers Also Viewed
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
N F Furlan et al.
The Journal of clinical pediatric dentistry, 37(1), 83-87 (2013-01-25)
Anxiety and stress are usually related to the dental treatment situation. The objective was to investigate salivary cortisol and alpha-amylase levels (salivary biomarkers) and heart rate in children undergoing a minor dental procedure (dental prophylaxis). In total, 31 children (range
Frederick J Warren et al.
Biochimica et biophysica acta, 1830(4), 3095-3101 (2013-01-09)
Starch is a main source of carbohydrate in human diets, but differences are observed in postprandial glycaemia following ingestion of different foods containing identical starch contents. Such differences reflect variations in rates at which different starches are digested in the
Elaheh Kashani-Amin et al.
FEBS letters, 587(6), 652-658 (2013-02-05)
Flavonoids and their precursor trans-chalcone have been reported as inhibitors of mammalian alpha-amylase. With regard to this background, neohesperidin dihydrochalcone (NHDC) effect was investigated toward porcine pancreatic alpha-amylase (PPA), and found to be an activator of the enzyme. The maximal
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service
