No abstract

A crude preparation of alkaline phosphatase (EC 3.1.3.1) from calf intestinal mucosa was purified by affinity chromatography on Sepharose-bound derivatives of arsanilic acid, which was found to be a competitive inhibitor of the enzyme. Three biospecific adsorbents were prepared for the chromatography, and the best results were obtained with a tyraminyl-Sepharose derivative coupled with the diazonium salt derived from 4-(p-aminophenylazo)phenylarsonic acid. Alkaline phosphatase was the only enzyme retained by the affinity column in the absence of Pi. The enzyme eluted by phosphate buffer had a specific activity of about 1200 units per mg of protein at pH 10.0, with 5.5mM-p-nitrophenyl phosphate as the substrate.

No abstract

No abstract

Commercial polyacrylonitrile was converted to the imidoester derivative and its capacity, degree of substitution and storage stability were tested.Urease, glucose oxidase and lactate dehydrogenase were coupled to the activated polymer by an amidino linkage. Some properties of the immobilized enzymes were studied and compared with those of the free enzymes.The use of enzymes bound to water-insoluble matrixes is an important branch of modern biotechnology. Many techniques have been developed so far for the immobilization of proteins onto polymers [l -31 and much work has been devoted to the preparation of an ideal matrix.