Journal ArticleDOI
The reactions between glutaraldehyde and various proteins. An investigation of their kinetics
D. Hopwood,C. R. Allen,M. McCabe +2 more
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The activation energies for the reactions between proteins and glutaraldehyde were found to be about II kcal/mole, which suggests that the proteins have not been denatured to any marked extent by the glutARaldehyde fixation.Abstract:
Glutaraldehyde reacts readily with various proteins in solution. With high concentrations of both, the solutions become yellow and many proteins form a gel. At low concentrations the reactions may be followed by the changes in the u.v. spectrum between 250 and 300 nm. The reverse reaction does not proceed to any detectable extent. The kinetics are pseudo-first-order. The activation energies for the reactions between proteins and glutaraldehyde were found to be about II kcal/mole. This suggests that the proteins have not been denatured to any marked extent by the glutaraldehyde fixation. The rates of reactions increase with pH. The rate of formation of glutaraldehyde-protein links per protein molecule glutarated is approximately I sec−1 mol−1 1.read more
Citations
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Journal ArticleDOI
Glutaraldehyde: behavior in aqueous solution, reaction with proteins, and application to enzyme crosslinking.
TL;DR: An overview of glutaraldehyde as a crosslinking reagent is given by describing its structure and chemical properties in aqueous solution in an attempt to explain its high reactivity toward proteins, particularly as applied to the production of insoluble enzymes.
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The role of glutaraldehyde-induced cross-links in calcification of bovine pericardium used in cardiac valve bioprostheses.
Gershon Golomb,Frederick J. Schoen,Mary Sue Smith,Judith A. Linden,Mark Dixon,Robert J. Levy +5 more
TL;DR: The amount of GLUT incorporated controls the extent of cross-links, which in turn directly determines tissue stability and calcification, in bovine pericardial tissue calcification.
Journal ArticleDOI
Theoretical and practical aspects of glutaraldehyde fixation.
TL;DR: The many structures put forward for glutaraldehyde, and the purification of the commercial material for chemical, histological and histochemical studies are considered, together with the physical changes in the proteins during the reactions.
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Antimicrobial activity, uses and mechanism of action of glutaraldehyde.
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Parameters in preparation and characterization of cross linked enzyme aggregates (CLEAs)
Sachin Talekar,Asavari Joshi,Gandhali Joshi,Priyanka Kamat,Rutumbara Haripurkar,Shashikant Kambale +5 more
TL;DR: The major parameters such as catalytic properties, particle size and morphology, stability and reusability required for approval of industrial applicability of newly synthesized CLEAs are critically reviewed.
References
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Journal ArticleDOI
Cytochemistry and electron microscopy. The preservation of cellular ultrastructure and enzymatic activity by aldehyde fixation.
TL;DR: A postfixation in osmium tetroxide, even after long periods of storage, developed an image that—notable in the case of glutaraldehyde—was largely indistinguishable from that of tissues fixed under optimal conditions with osmia tetroxides alone.
Book ChapterDOI
Ultraviolet spectra Of Proteins and Amino Acids
TL;DR: This chapter reviews that the simplest way of accounting for the absorption spectrum of a protein is as the sum of the spectra of its components, and discusses that the failure of perfect additivity of the component absorptivities affords the possibility of obtaining structural information about proteins.
Journal ArticleDOI
Glutaraldehyde as a protein cross-linking reagent
Journal ArticleDOI
XLVI. On the determination of the velocity constant of a unimolecular reaction
TL;DR: In this article, the determination of the velocity constant of a unimolecular reaction is discussed. But the authors focus only on the case where the reaction can be seen as a single particle.
Journal ArticleDOI
Reaction of Proteins with Glutaraldehyde
A.F.S.A. Habeeb,R. Hiramoto +1 more
TL;DR: Glutaraldehyde was found to react with the α-amino groups of amino acids, the N-terminal amino groups of some peptides and the sulfhydryl group of cysteine, and the phenolic and the imidazole rings of tyrosine and histidine derivatives were partially reactive.