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The Masson staining of collagen — an explanation of an apparent paradox (1975)

Flint, Michael H. ; Lyons, Mary F. ; Meaney, M. F. ; [et al.]

Springer

Journal of molecular histology 7 (1975), S. 529-546

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ISSN: 1573-6865

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Medicine

Notes: Synopsis Although collagen of either tendon or dermis can be stained equally well with Ponceau 2R/Acid Fuchsin or Light Green SF if the dyes are used independently, tendon collagen retains the red dye mixture and dermal collagen the green counterstain when the dyes are used sequentially in the Masson trichrome procedure. The results of experiments designed to assess differences in the penetration, retention and displacement of these arylmethane dyes have demonstrated that they are retained more firmly by the tensioned collagen of tendon or stretched dermis, and are more easily displaced from the collagen of relaxed tendon or dermis. Experiments designed to test the basis of these differences in dye retention indicate that more positively-charged amino dye-binding sites are available in the tensioned collagen than in relaxed collagen, where they appear to be closely associated with adjacent carboxyl groups on the collagen fibres. The possibility that the carboxyl groups of associated acid mucopolysaccharides are implicated in the differences in staining propensity has been investigated and discounted. It is suggested that whereas the binding of arylmethane dyes to collagen under tension is through strong ionic linkages to amino groups, the binding of these and other dyes to relaxed collagen is through weaker hydrogen bonds. It is proposed that these differences in charge distribution on the collagen of the two situations is related to the previously described piezo-electric effect demonstrable on stretched collagen.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF01003791

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The effect of heating and denaturation on the staining of collagen by the Masson trichrome procedure (1975)

Flint, Michael H. ; Lyons, Mary F.

Springer

Journal of molecular histology 7 (1975), S. 547-555

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ISSN: 1573-6865

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Medicine

Notes: Synopsis Although normally, dermal collagen fails to retain the Ponceau 2R/Acid Fuchsin component of the Masson trichrome procedure and is stained green by the counterstain, the collagen of sections of human dermis which have been heated above its denaturation temperature (T s) in moist conditions will retain the initial red stain. This difference in dye retention appears to be related to conformational changes of the collagen molecule which are associated with denaturation, for the change in staining is directly related to the shrinkage temperature, is reversed by rapid cooling after heating, is profoundly affected by differences in environmental conditions during heating which affect molecular rearrangement, and is age-dependent. Analogous changes in staining propensity have been observed in heated keratin and epidermis. However, whereas the retention of the initial red dye mixture is increased in denatured dermis, it is diminished in heated epidermis. It is suggested that the subtle dye substrate interaction of the Masson trichrome staining procedure can be utilized to demonstrate changes in molecular configuration which are associated with thermal, as well as other forms of denaturation of collagen and other proteins.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF01003792

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