Aldehyde metabolism in the human lens.

From studies involving 31 cataracts classified by the CCRG system and eight normal human lenses, it has been found that the adult human lens contains an enzyme system capable of oxidizing 1-2 mumol of glyceraldehyde, acetaldehyde, propionaldehyde, formaldehyde, and malonaldialdehyde per hour to their carboxylic acid form. Roughly 30 mumol G-3-P can be oxidized per hour. Statistically, the level of the oxidase system in nuclear cataracts and deeply pigmented lenses was found to be the same as for normal lenses. The deficiency of an enzyme responsible for the oxidation of highly reactive aldehydes thus seems unlikely to be involved in nuclear cataract formation and the browning of the lens. Evidence that the observed oxidase activity occurs via two separate enzymes: aldehyde dehydrogenase and glyceraldehyde-3-P dehydrogenase was achieved by studying the response of enzyme to substrate and activators (dithiothreitol and arsenate) and by final separation of enzyme activities. Differences in pH optima and heat treatment response further distinguished one enzyme from the other.

An in vivo study of an antimicrobial mouth rinse on supragingival and subgingival plaque and calculus formation.

An antibiotic mouth rinse (CC10232) was used twice a day for one week in human subjects in a supervised double blind clinical and histological study. Nylon strips were placed supra and subgingivally for one week and then sectioned, stained and examined. Results showed that the rinse containing CC-10232 reduced the amount of plaque and reduced the amount of mineralization in 4 of 5 subjects.Also, no spirochetes were found in subjects who utilized this rinse.