Alpha neoprotein molecules in normal lenses from animals of different ages and in cataractous lenses

Alpha neoprotein molecules are formed by an association of A and B subunits resulting in a different quaternary structure than in alpha crystallin. The content of alpha neoprotein vs. alpha crystallin was estimated separately on the crystallin, cryoprotein and albuminoid fractions in lenses of animals of different species and ages, in lenses with experimentally induced cataracts and in human cataractous lenses. Alpha crystallin was determined on immunoadsorbents with bound antibodies restricted to quaternary determinants of this protein. Alpha neoprotein molecules were determined in the filtrate containing lens proteins not bound on the above immunoadsorbent. The filtrate was applied on an anti-A chain immunoadsorbent, and after desorption the A chain-containing molecules were applied on an anti-B chain immunoadsorbent. The amount of lens proteins bound to the latter immunoadsorbent gave a measure of molecules formed by an association of A with B chains other than in alpha crystallin, that is of alpha neoproteins. No alpha neoprotein was present in lenses from 2-week-old rats or in the 3- to 6-month-old calf lens cortex. The 2-year-old bovine lens nucleus did contain alpha neoproteins, but only in the albuminoid fraction. The lenses of adult rats (i.e. 3- to 4-month-old) contained alpha neoprotein molecules mainly in the albuminoid fraction; small amounts were also found in the cryoprotein fraction. All three fractions of lens proteins from 1-year-old rats contained alpha neoprotein molecules. No significant differences in the content of alpha neoprotein molecules were found in lenses with experimentally induced X-ray and galactose cataracts and in normal controls. This finding does not exclude possible structural differences between normal and cataractous alpha neoproteins. In human senile cataractous lenses, the content of alpha neoprotein molecules in all fractions analyzed equaled or exceeded the content of alpha crystallin present. The present findings demonstrate an age-dependent formation in the mammalian lens of alpha crystallin neoproteins lacking native quaternary determinants. The data obtained point to the possibility that the structural lability of alpha crystallin may be a contributing factor in cataractogenesis.