Amylase is an enzyme that breaks starch down into sugar. Amylase is present in human saliva, where it begins the chemical process of digestion. Foods that contain much starch but little sugar, such as rice and potato, taste slightly sweet as they are chewed because amylase turns some of their starch into sugar in the mouth. Alpha-Amylase is an enzyme that hydrolyses alpha-bonds of large alpha-linked polysaccharides such as starch and glycogen, yielding glucose and maltose. It is being used by researchers as a barometer of the bodys response to physical or psychological stress. NIH study shows that women with high levels of alpha amylase, indicating stress, are less likely to conceive. Source: Human Saliva CAS No: 9000-90-2 E.C. No: 3.2.1.1 Activity: >100 U/mg (Siemens Dimension Clinical Chemistry System) Specific Activity: > 400 U/mg protein Unit Definition: One unit will catalyze the hydrolysis of one micromole 2-chloro-4-nitrophenyl-a-D-maltotrioside to yield 2-chloro-4-nitrophenol/minute at 37C. Protein: > 0.2 mg protein/mg (Coomassie) Contaminants: Lipase: < 0.05% Protease: < 0.1% Ammonia: < 0.1 micromole/mg pH: 6.0 - 7.5 (10mg/ml, H2O) Form: Lyophilized from Tris Chloride, Mannitol pH 7.2 Appearance: White to off-white powder Solubility: Clear, colorless (10 mg/mL saline) Reconstitution: Reconstitute with saline at 100 units/mL. Further dilutions should be in the lyophilization buffer (75mM sodium chloride, 10mM tris chloride, 1mM calcium chloride, pH 7.2) or a similar solution. Calcium is important for the best activity and stability. Storage and Stability: Lyophilized and reconstituted products are stable for 6 months after receipt at -20C. Reconstitute with sterile ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
