We automated a kinetic procedure for determining amylase isoenzymes in serum and urine samples. We used 4-nitro-phenylmaltoheptaoside as substrate and a selective amylase inhibitor with the Abbott-VP bichromatic system. By use of the maximum differences between pancreatic (P) and salivary (S) amylase activities remaining after inhibition by the selective inhibitor and by use of the linear range...

An electrophoretic transfer technique was developed for the specific identification of isozymes of starch debranching enzyme, alpha-amylase, and beta-amylase. Amylolytic enzymes are separated by native polyacrylamide slab gel electrophoresis and proteins in gels are electrophoretically transferred through starch-containing polyacrylamide gels. Each amylolytic enzyme degrades starch in the trans...

The research included isolation and purification of Trypsin from serum patient with pancreatic cancer, estimation its molecular weight by using the two techniques gel filtration (using sephadex G-50) electrophoresis SDS). Therefore; it was noted that proteinous peak isolated ammonium sulfate solution is saturated (65%) had apparent (27000) Dalton. study (40) patients pancreas cancer their ages ...

Starch, total amylolytic and phosphorylase activities were determined in lentil cotyledons during the first days of germination. Several independent criteria show that the amylolytic activity is due mainly to an amylase of the alpha type. Starch is degraded slowly in the first days; during this time, alpha- and beta-amylase activity are very low, while phosphorylase increases and reach a peak o...

To evaluate a new method for measuring pancreatic amylase in serum, in which the salivary isoenzyme is inhibited with a specific monoclonal antibody, we determined the activity of pancreatic and salivary amylase in sera from 103 healthy subjects and from 114 hospitalized patients having a wide range of total amylase activities. CVs for the proposed method ranged from 0.8% to 5.1% (within day) a...

We describe a new method for measuring pancreatic and salivary-type amylases in serum that requires no electrophoresis or chromatography. An inhibitor protein (from wheat) with a 100-fold greater specificity for human salivary than for human pancreatic amylase was used to analyze mixtures of the two enzymes. The concentration of pancreatic and salivary amyalase was determined in 141 normal sera...

Enzymes produced by microorganisms and plants are used as food additives to aid the processing of foods. Identification of the origin of these enzyme products is important for their proper use. Proteinase digestion of α-amylase products, followed by high performance liquid chromatography (HPLC) analysis, was applied to α-amylase from the mold Aspergillus species, the bacteria Bacillus species, ...

Evaluation of a-amylase isoenzymes as a clinical diagnostic aid by previous methodologies has been either too insensitive or too cumbersome for routine clinical laboratory use. With use of an agarose gel electrophoresis system (Worthington Diagnostic Systems, Inc.) serum amylase activity can easily be resolved into at least nine isoenzymes, the resolution being comparable with that of isoelectr...

Human salivary amylase and pancreatic amylase were purified and characterized. These amylases gave two bands and one band, respectively, each staining for both protein and sugar, after electrophoresis on sodium dodecyl sulfate--polyacrylamide gel. The relative molecular mass (Mr) or pancreatic amylase was calculated to be 60 000; for the two components (A and B) of salivary amylase the Mr were ...

Investigations were made concerning the number and properties of amylase in sugarcane leaves. Enzymes were extracted froin leaf samples which had been frozen, lyophilized, and ground to a fine powder. Techniques of differential solubihty, gel filtiation, and papei electrophoresis were employed to remove amylase from the crude extracts. Solubility studies showed that amylase was moderately preci...