Reaction of Certain Aliphatic Aldehydes with Gelatin

Ra, Milch

doi:10.1159/000211399

Cited by 17 publications

(2 citation statements)

References 18 publications

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“…Since glutaraldehyde fixation was found to be essential for the preservation and visualization of the protein structure, it seems likely that a chemical alteration of the protein had occurred. This could involve intramolecular and/or intermolecular linkages between amino, amide, or guanidyl groups on the proteins which stabilize the associations of adjacent units (20). The arrangement of the lipids within these spacings, whether globular or lamellar, cannot be directly deduced from our studies.…”

Section: Discussionmentioning

confidence: 91%

Preservation of Myelin Lamellar Structure in the Absence of Lipid

Napolitano

LeBaron

Scaletti

1967

The Journal of Cell Biology

117

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The fine structure of myelin was studied in glutaraldehyde-fixed rat sciatic nerves depleted of lipid by acetone, chloroform:methanol (2:1 v/v), and chloroform:methanol:concentrated HC1 (200:100:1, v/v/v). One portion of each of these nerves, plus the extracts, was saponified and analyzed by gas-liquid chromatography for fatty acids. The remainder of each nerve was stained in osmium tetroxide in CC1 4 (5g/100cc) and was embedded in Epon 812. Thin sections, examined in the electron microscope, revealed the preservation of myelin lamellar structure with a 170 A periodicity in nerves depleted of 98% of their lipids. Preservation of myelin lamellar structure depended on glutaraldehyde fixation and the introduction of osmium tetroxide in a nonpolar vehicle (CC14) after the lipids had been extracted. It is concluded that the periodic lamellar structure in electron micrographs of myelin depleted of lipid results from the complexing of osmium tetroxide, plus uranyl and lead stains, with protein.

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Section: Discussionmentioning

confidence: 91%

Preservation of Myelin Lamellar Structure in the Absence of Lipid

Napolitano

LeBaron

Scaletti

1967

The Journal of Cell Biology

117

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“…Substantially equal in rapidity in crosslinking proteins and nucleic acids are the other aldehydes which are water‐soluble monomeric C 1 to C 3 aliphatic mono‐aldehydes and C 2 to C 5 di‐aldehydes; these have an electrophilic substitution on the alpha C atom, and an unsubstituted terminal hydrogen atom (Gustavson, 1949; Milch, 1964). These include several metabolically active aldehydes such as glyoxal, glyceraldehyde, and pyruvaldehyde, in addition to those already mentioned.…”

Section: Presence Of Crosslinking Agents In the Living Organismmentioning

confidence: 99%

The Crosslinkage Theory of Aging

Bjorksten

1968

J American Geriatrics Society

142

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For many decades the theory and practice of cross‐linking (bonding that ties two or more large molecules together side to side) have been developed in industry, but only since the 1940's has the theory been considered in the field of medicine as a primary reaction underlying age‐dependent changes. Crosslinking is damaging to the tissues and involves loss of elasticity, reduced swelling capacity, increased resistance to hydrolases and probably enzymes generally, and thus an increase in molecular weight and a tendency toward embrittlement. There is a growing amount of direct evidence and much indirect evidence for postulating the relationship between crosslinking and aging. Crosslinking agents present in the living organism include aldehydes, lipid oxidation products, sulfur, alkylating agents, quinones, free radicals induced by ionizing radiation, antibodies, polybasic acids, polyhalo derivatives and polyvalent metals. The latter four types of compound are slow‐acting but can also accumulate in the body to form a frozen metabolic pool. Sufficient amounts of all these potential crosslinking materials are present in the body to make the changes of aging unavoidable.

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The interaction of glutaraldehyde with poly(α,L‐lysine), n‐butylamine, and collagen. II. Hydrodynamic, electron microscopic, and optical investigations on the reaction products

et al. 1975

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SynopsisInteractions of glutaraldehyde with either n-butylamine, poly(a,L-lysine), or collagen resulted in a fast release of protons in dilute aqueous solutions a t various pH values, followed by much slower changes. The latter reactions, which extended over hours and days, were followed spectrophotometrically and revealed the formation of distinct absorption bands in the visible and near-ultraviolet regions in all the above systems. The visible-range bands disappeared upon treatment with sodium borohydride. A qualitative relationship between oxygen uptake by the system n-butylamine-glutaraldehyde and the slow formation of colored products has been established, while the chemical nature of the reaction products has not been determined.Sedimentation velocity, viscosity, and optical rotation measurements on the products of interaction between poly(L-lysine) and glutaraldehyde in aqueous solution indicated large conformational changes in the polyamino acid present in excess (in residues) over the dialdehyde. In particular, the intrinsic viscosity dropped considerably after interaction, indicating intramolecular crosslinking. At molar ratios of 1:1 between polylysine residues and aldehyde groups, intermolecular crosslinking of polylysine was obtained a t pH 8.6.Electron microscopic examidations of collagen samples treated by glutaraldehyde a t various pH values indicated changes from unordered to more ordered structures upon treatment with glutaraldehyde, in particular a t pH 10.The present structural and optical investigations are considered to be relevant to tanning processes of hides and to fixation procedures.

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Reaction of Certain Aliphatic Aldehydes with Gelatin

Cited by 17 publications

References 18 publications

Preservation of Myelin Lamellar Structure in the Absence of Lipid

Preservation of Myelin Lamellar Structure in the Absence of Lipid

The Crosslinkage Theory of Aging

The interaction of glutaraldehyde with poly(α,L‐lysine), n‐butylamine, and collagen. II. Hydrodynamic, electron microscopic, and optical investigations on the reaction products

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