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Properties of ribulose diphosphate carboxylase immobilized on porous glassRibulose-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.
Document ID
19750043003
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
External Source(s)
Authors
Shapira, J.
Hanson, C. L.
Lyding, J. M.
(NASA Ames Research Center Moffett Field, Calif., United States)
Reilly, P. J.
(Nebraska, University Lincoln, Neb., United States)
Date Acquired
August 8, 2013
Publication Date
January 1, 1974
Publication Information
Publication: Biotechnology and Bioengineering
Volume: 16
Subject Category
Chemistry And Materials (General)
Accession Number
75A27075
Distribution Limits
Public
Copyright
Other

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