Access the full text.
Sign up today, get DeepDyve free for 14 days.
The Ultra - violet Absorption of Protein - Bound Glutaraldehyde
D. Speer, M. Chvapil, ROBERT Vorz, MICHAEL Holmes (1979)
Enhancement of healing in osteochondral defects by collagen sponge implants.Clinical orthopaedics and related research, 144
P. Hardy, A. Nicholls, H. Rydon (1969)
The nature of glutaraldehyde in aqueous solutionJournal of The Chemical Society D: Chemical Communications
(1965)
Determination of Formaldehyde and Glutaraldehyde Bound to Collagen by Carbon - 14 Assay
A. H. Korn, E. M. Filachione (1967)
The Direct Determination of Bound Glutaraldehyde in Glutaraldehyde‐Tanned Collagen. Determination of Bound Glutaraldehyde, 62
F. Cervinka, M. Krajicek (1964)
Notes on the Problem of Antigenicity of Collagen, 10
J. Bowes, C. Cater (1965)
Crosslinking of collagenJournal of Chemical Technology & Biotechnology, 15
F. Červinka, M. Krajíček, M. Liška, J. Vrubel (1964)
NOTES ON THE QUESTION OF THE ANTIGENICITY OF COLLAGEN.Folia biologica, 10
M. Chvapil, T. Chvapil, J. Owen, K. Keown (1978)
Reaction of vaginal tissue of rabbit and of cheek pouch of hamster to inserted collagen sponges treated with either zinc or copper.American journal of obstetrics and gynecology, 130 1
E. Chang, J. Chien (1973)
Optical characterization of orientation of collagenBiopolymers, 12
C. Thies, S. Cuthbertson, N. Yoshida (1968)
The reaction of glutaraldehyde with dilute solutions of an acid-precursor gelatinJournal of Colloid and Interface Science, 27
F. Richards, J. Knowles (1968)
Glutaraldehyde as a protein cross-linking reagentJournal of Molecular Biology, 37
N. C. Rath, A. H. Reddi (1979)
Collagenous Bone Matrix is a Local Mitogen, 278
M. Swenson, E. Meir, P. Yanai, B. Zvilichovsky, G. Blauer (1975)
The interaction of glutaraldehyde with poly(α,L‐lysine), n‐butylamine, and collagen. II. Hydrodynamic, electron microscopic, and optical investigations on the reaction productsBiopolymers, 14
William Harrington, Peter Hippel (1961)
The structure of collagen and gelatin.Advances in protein chemistry, 16
W. Mcmaster, Jack Kouzelos, Shardon Liddle, T. Waugh (1976)
Tendon grafting with glutaraldehyde fixed material.Journal of biomedical materials research, 10 2
C. Aso, Yuzo Aito (1962)
Studies on the polymerization of bifunctional monomers. II. Polymerization of glutaraldehydeMacromolecular Chemistry and Physics, 58
(1961)
The Effect of Tanning Agents on the Optical Birefringence of Collagen
M. Chvapil, C. Kischer, J. Campbell, M. Kantor, J. Owen, T. Chvapil (1978)
Ultrastructure of the vaginal tissue of rabbits treated with collagen sponge alone and medicated with zinc and copper salts and copper wire.Fertility and sterility, 30 4
E. M. Filachione, A. H. Korn, J. S. Ard (1967)
Technical Notes. The Ultraviolet Absorption of Protein‐Bound Glutaraldehyde, 62
A. Everson (1953)
Histochemistry: Theoretical and AppliedMedical Journal of Australia, 1
R. Allen (1964)
Image Contrast and Phase Modulated Light Methods in Polarization and Inteference Microscopy. Instruction Manual for the PAR EPM-1 Photoelectric Polarizing and Interference Microscope
E. A. Woodroof (1978)
Use of Glutaraldehyde and Formaldehyde to Process Heart Valves, 2
P. Anderson (1967)
PURIFICATION AND QUANTITATION OF GLUTARALDEHYDE AND ITS EFFECT ON SEVERAL ENZYME ACTIVITIES IN SKELETAL MUSCLEJournal of Histochemistry and Cytochemistry, 15
J. Bowes, C. Cater (1966)
The reaction of glutaraldehyde with proteins and other biological materialsJournal of The Society of Dyers and Colourists, 85
E. Woodroof (1978)
Use of glutaraldehyde and formaldehyde to process tissue heart valves.Journal of bioengineering, 2 1-2
G. Blauer, D. Harmatz, E. Meir, M. Swenson, B. Zvilichovsky (1975)
The interaction of glutaraldehyde with poly(α,L‐lysine), n‐butylamine, and collagen. I. The primary proton release in aqueous mediumBiopolymers, 14
R. Cox, R. Grant, C. Kent (1973)
An electron-microscope study of the reaction of collagen with some monoaldehydes and bifunctional aldehydes.Journal of cell science, 12 3
R. Grant, R. Cox, C. Kent (1970)
Electron microscope studies of deaminated and crosslinked collagenJournal of Microscopy, 92
E. Slayter (1970)
Optical methods in biology
Glutaraldehyde is commonly used to control physical and biological properties of collagen structure by means of intramolecular and/or intermolecular crosslinking of collagen molecules. Solubility, antigenicity, and biodegradation of naturally occurring or reconstituted collagenous matrices are effectively reduced by glutaraldehyde treatment. Adverse biological reactions to glutaraldehyde have been limited to infrequent contact dermatitis and to biocidal effects which are exploited in chemical sterilization media. In the present study of glutaraldehyde‐tanned collagen sponge, the presence of glutaraldehyde was correlated with cytotoxic effects upon fibroblasts in tissue culture and foreign body giant cell reaction to bioimplants of the sponge. Fibroblast growth in tissue culture is 99% inhibited at media concentrations of 3.0 ppm glutaraldehyde. Extracts of glutaraldehyde collagen sponge in aqueous media at pH 7 and 4.5 yielded 6 μg and 65 μg glutaraldehyde per gram of collagen sponge, respectively. The yield increased tenfold at pH 4.5. Observations indicate that leaching of the glutaraldehyde from glutaraldehyde‐tanned collagen sponge is sufficient to produce potentially adverse cellular effects both in vivo and in vitro.
Journal of Biomedical Materials Research Part A – Wiley
Published: Nov 1, 1980
Read and print from thousands of top scholarly journals.
Already have an account? Log in
Bookmark this article. You can see your Bookmarks on your DeepDyve Library.
To save an article, log in first, or sign up for a DeepDyve account if you don’t already have one.
Copy and paste the desired citation format or use the link below to download a file formatted for EndNote
Access the full text.
Sign up today, get DeepDyve free for 14 days.
All DeepDyve websites use cookies to improve your online experience. They were placed on your computer when you launched this website. You can change your cookie settings through your browser.