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Properties of ribulose diphosphate carboxylase immobilized on porous glass
Author(s) -
Shapira Jacob,
Hanson Carl L.,
Lyding Judith M.,
Reilly Peter J.
Publication year - 1974
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260161107
Subject(s) - dithiothreitol , porous glass , glutaraldehyde , diazo , spinach , chemistry , ribulose , pyruvate carboxylase , enzyme , biochemistry , chromatography , porosity , organic chemistry
Ribulose‐1,5‐diphosphate carboxylase from spinach has been bound to arylamine porous glass with a diazo linkage and to alklamine porous glass with glutaraldehyde. Stability at elevated temperatures and responses to changes of pH and ribulose‐1,5‐diphosphate, Mg 2+ , and dithiothreitol concentrations were not significantly different from the soluble enzyme, though stability at 4°C was somewhat improved.