background: today a large number of bacterial amylases are available commercially in industry. the goal of the present study was purification and biochemical characterization of an extracellular thermostable alkaline α-amylase from the novel moderately halophilic, bacillus persicus from the aran-bidgol, iran.   methods : purification of enzyme, was carried out by acetone precipitation, ultrafil...

Alkaline phosphatase prepared from mammalian cell cultures was found to have alkaline inorganic pyrophosphatase activity. Both of these activities appear to be associated with a single protein, as demonstrated by: (1) concomitant purification of alkaline phosphatase and alkaline inorganic pyrophosphatase; (2) proportional precipitation of alkaline phosphatase and inorganic pyrophosphatase activ...

The various purification methods have been developed to improve the quality local salt, NaCl content > 94%. Bentonite is one of materials used as binder impurities in purification. purpose study was synthesis a modified bentonite using alkaline solution, which includes natrium hydroxide (NaOH) and potassium (KOH) with concentrations (1, 1.5, 2, 2.5 M) determined level Na+, Ca2+ Mg2+ metals A...

A rapid and improved method to obtain purified lactase from rat intestine is described. The purification procedure involved only two chromatographic steps. The degree of purification was far above (500 fold) the values reached with classical methods. Rabbit antisera raised to the purified lactase were characterized using conventional immunological techniques. The specificity of the lactase anti...

In a previous communication (Li, H.-C., Hsiao, K.-J., and Chan, W. W. S. (1978) Eur. J. Biochem 84,215-225) we reported the purification of a divalent cation-independent, nonspecific phosphoprotein phosphatase (phosphatase S, M, = 35,000) from canine cardiac muscle to apparent homogeneity. It was found that the homogeneous enzyme preparation exhibited significant activity toward p-nitrophenyl p...

Purification, molecular weights, amino acid compositions, and partial sequencing of intestinal alkaline phosphatases (EC 3.1.3.1) from human adult, human fetal, and bovine sources is reported. Additional sequence information is presented for the bovine liver isozyme. Comparisons are made of the partial primary structures of intestinal alkaline phosphatases with those of the isozymes from liver ...