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Proteins coupled to polyacrylamide beads using glutaraldehyde

Authors
Journal
Biochemical and Biophysical Research Communications
0006-291X
Publisher
Elsevier
Publication Date
Volume
45
Issue
6
Identifiers
DOI: 10.1016/0006-291x(71)90200-2
Disciplines
  • Biology

Abstract

Abstract Optimum conditions were determined for linking acid phosphatase to polyacrylamide beads using glutaral dehyde, and the method was extended to other proteins. The enzyme activity retained by the covalently bound protein was more than 55 % for acid phosphatase, glucose oxidase, trypsin and chymotrypsin. The stability of the enzyme-polyacrylamide gel conjugates was tested during heating, freeze-drying, and storage at 4° C.

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