Summary
Sulfation and methylation-sulfation induces proteolytic sensitivity in formolfixed paraffin sections of fibrillary collagen and basement membranes. Other fibrillary elements such as myofibrils, tonofibrils and fibrin as well as the cell elements of connective and parenchymatous tissues are resistant in methylated sulfated sections and remain well preserved after enzyme incubation. Since desulfation of the sulfated sections abolished the sulfation-induced proteolytic sensitivity of collagen and basement membranes it was obvious that the sensitivity was not the result of non-specific structural damage caused by the sulfation procedure.
On the analogy of the selective proteolytic sensitivity of acetyl collagen it is assumed that in sulfate-collagen the proteolytic sensitivity depends on the sulfate esterification of the OH groups. Blocking of the vicinal OH groups of carbohydrates by periodic acid did not induce proteolytic sensitivity in collagen or basement membranes. Sulfation-induced selective collagenolysis provides a new insight into many facts of structural organisation of tissues.
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Romhányi, G., Bukovinszky, A. & Deák, G. Selective proteolytic sensitivity of sulfate-collagen and basement membranes. Histochemistry 42, 199–209 (1974). https://doi.org/10.1007/BF00533271
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DOI: https://doi.org/10.1007/BF00533271