Five major crystallin fractions were found in camel lens fractionated by Sepharose CL-6B column chromatography. These crystallin fractions were named alpha high (αH), alpha low (αL), beta high (βH), beta low (βL) and gamma (γ) by comparison with the elution profiles and molecular weights of rabbit crystallins. The amino acid composition and isoelectric focusing bands for crystallins of camel and rabbit were remarkably similar, but individual differences were found. By means of sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), two alpha H crystallin subunits, of 23K and 20K molecular weight, were found in camel and rabbit. Likewise, a single 21K molecular weight band was found in the gamma crystallin of camel and rabbit. In camel, the beta high crystallin consisted of five major subunits, while rabbit beta high crystallin consisted of only three subunits. On SDS-PAGE, camel and rabbit beta low crystallins both showed two major subunits of 27K and 23K molecular weight but camel beta low crystallin showed an additional 35K molecular weight subunit. Characterization of camel lens crystallins may contribute to understanding the effect of aging on aggregation of camel crystallins.