Literature DB >> 1710883

Entrapment of proteins by aggregation within sephadex beads.

S K Khare1, S Vaidya, M N Gupta.   

Abstract

When a protein is aggregated by chemical crosslinking inside Sephadex beads of appropriate pore size, it gets trapped inside the beads. The above approach was used for immobilization of beta-galactosidase, acid phosphatase, trypsin, and concanavalin A. It was found to be a simple, convenient, and fast method for immobilization of proteins.

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Year:  1991        PMID: 1710883     DOI: 10.1007/bf02921536

Source DB:  PubMed          Journal:  Appl Biochem Biotechnol        ISSN: 0273-2289            Impact factor:   2.926


  4 in total

1.  Coaggregate of trypsin and chymotrypsin.

Authors:  Y S Rajput; M N Gupta
Journal:  Biotechnol Bioeng       Date:  1988-02-20       Impact factor: 4.530

2.  Crosslinked concanavalin A-O-(diethylaminoethyl)-cellulose--an affinity medium for concanavalin A-interacting glycoproteins.

Authors:  A Kamra; M N Gupta
Journal:  Anal Biochem       Date:  1987-08-01       Impact factor: 3.365

3.  Isolation of three acid phosphatases from wheat germ.

Authors:  Z H Verjee
Journal:  Eur J Biochem       Date:  1969-06

4.  Immobilization of E. coli beta-galactosidase and its derivatives by polyacrylamide gel.

Authors:  S K Khare; M N Gupta
Journal:  Biotechnol Bioeng       Date:  1988-05-20       Impact factor: 4.530

  4 in total

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