Abstract
Rat aortic elastin contains a non-periodic acid-engendered aldehyde that reacts with either conventional pH 2.5 Schiff's reagent or a Schiff's reagent of pH 6.7. The elastin of animals 20 and 40 days old was colored a vivid purple-red, whereas the elastin from 18-mo-old animals was not stained. Elastin from the young animals when subjected to aldehyde blockage prior to HIO4 oxidation was not stained. Histochemical and biochemical literature of the past 10 yr pertinent to Schiff and periodic acid-Schiff reactivity with elastin indicate that an intermediate compound, α-amino adipic-δ-semialdehyde, formed during the conversion of lysin to one of several cross linking amino acids found in elastin, is the source of the aldehyde responsible for the direct Schiff reaction.