Properties of ribulose diphosphate carboxylase immobilized on porous glass | Zendy

Shapira Jacob | Zendy; Hanson Carl L. | Zendy; Lyding Judith M. | Zendy; Reilly Peter J. | Zendy

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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.

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