Immobilized ribonuclease and alkaline phosphatase

Textiles: fiber preparation

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195 63, 195 68, 195DIG11, 195116, C07G 702, C12B 100

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active

040393828

ABSTRACT:
An insoluble, solid matrix carrying simultaneously several different enzymatic functions, is constituted by the conjoint association by irreversible binding on a previously activated matrix support, of a nuclease selected from the group of ribonucleases A, T.sub.1, T.sub.2, U.sub.2 and an alkaline phosphatease. Free activated groups of the matrix after binding of the enzymes, are neutralized by a free amino organic base. The support is selected from among non-denaturing supports effecting the irreversible physical adsorption of the enzymes, such as supports of glass or quartz beads, highly cross-linked gels of the agarose or cellulose type. Polymers A.sub.n U.sub.OH, A.sub.n C.sub.OH, A.sub.n G.sub.OH and/or oligonucleotides U, C, A or G, of predetermined lengths, can be obtained by fractionating the polyribonucleotides by incubation with the insoluble solid matrix.

REFERENCES:
lee, J. C., Preparation and Properties of Water Insoluble Derivatives of Ribonuclease Ti. Biochim. Biophys. Acta., vol. 235, 1971, (pp. 435-441).
Woetall, H. H., Alkaline Phosphatase Insolubilized by Covalent Linkage to Porons Glass., Nature., vol. 223, 1969, (pp. 959-960).
Hultin, H. O., Characteristics of Immobilized Multi-Enzyme Systems, Journal of Food Science, vol. 39, 1974, (pp. 647-652).
Zaborsky, O., Immobilized Enzymes, CRC Press, Cleveland, Ohio, 1973, (pp. 124-126).

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