ISSN:
0021-9304
Keywords:
Chemistry
;
Polymer and Materials Science
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Medicine
,
Technology
Notes:
ATP-diphosphohydrolase, trypsin, and chymotrypsin have been insolubilized by lattice-entrapment using hydrophilic polyacrylamide gel and hydrophobic Silastic matrices. The entrapped enzymes were stable and unaffected by washing or wet storage. Thermal inactivation properties of polyacrylamide-entrapped ATP-diphosphohydrolase were different from those of the same enzyme in solution. Several substrates were used for each of the proteolytic enzymes. Esterase activities of both trypsin and chymotrypsin were unaltered by entrapment within Silastic. The entrapment of enzymes and other active proteins is potentially of consequence in continuous-flow substrate conversion systems. Silastic with a surface proteolytic activity derived from an entrapped enzyme is of possible medical utility for implantation elements.
Additional Material:
3 Tab.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/jbm.820020206
Permalink