Abstract
PREVIOUS publications from this laboratory have demonstrated that specific hydrated aliphatic aldehydes1,2 react both in vitro and in vivo3–5 with the freely rotatable nitrogen atoms6 of native and ‘purified’ collagen and elastin chains. The resulting products are highly cross-linked network structures7 which are characterized by ‘locking-in’ of dipoles8 normally present along the respective polypeptide chains. Unfortunately, little is known about the quantitative aspects of the involved reactions. The presently reported investigation was accordingly prompted, in which the binding of two specific C3 aldehydes to hide powder collagen, extracted aortic elastin, intact (control) bovine thoracic aortae and sonicated bovine thoracic aorta preparations were investigated.
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