Journal Article10.1016/0022-2836(68)90086-7
Glutaraldehyde as a protein cross-linking reagent
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About: This article is published in Journal of Molecular Biology. The article was published on 14 Oct 1968. The article focuses on the topics: Glutaraldehyde & Reagent.
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Citations
Biochemical changes and cytotoxicity associated with the degradation of polymeric glutaraldehyde derived crosslinks.
TL;DR: The chemical and biological studies suggest that local cytotoxicity of glutaraldehyde crosslinked bioprostheses may be due to unstable glutarhyde polymers that persist in the interstices of crosslinked tissues.
336
•Journal Article
Biologic determinants of dystrophic calcification and osteocalcin deposition in glutaraldehyde-preserved porcine aortic valve leaflets implanted subcutaneously in rats.
TL;DR: Examining the biologic determinants of this type of dystrophic calcification using subcutaneous implants of glutaraldehyde-preserved porcine aortic valve leaflets in rats found that GPVs calcified progressively, with mineral deposition occurring in a morphologic pattern comparable to that noted in clinical retrievals.
307
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.
291
The chemistry of enzyme and protein immobilization with glutaraldehyde
David R. Walt,Venetka I. Agayn +1 more
TL;DR: The structure and reactivity of glutaraldehyde protein immobilization is detailed, which shows a complex chemistry that is transparent to most practitioners of immobilization.
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References
The Mechanism of Hydrolysis of Schiff Bases Derived from Aliphatic Amines
E. H. Cordes,W. P. Jencks +1 more
TL;DR: Ultraviolet spectrum in methanol: 6~-Nitro-3~,5~-cycloandrostan-17-one (XVII)29 (Fig. 16): C.R.D. in methangl ( c 0.0474, 280 -240 mp): [+I311 -7950 , [+]305 -8030 , +P500).
289
Isoelectric point of a protein in the crosslinked crystalline state: β-Lactoglobulin☆
TL;DR: Titration in 2 m -KCl of a suspension of crosslinked crystals from pH 2 to 12 indicates no change in the number of dissociable groups when compared with solution behavior, and close correspondence of the curves acid to pH 6.2 suggests the 27 lysyl residues modified by the crosslinking reaction appear merely to have had their pK′ values lowered.