PURIFICATION AND SOME PROPERTIES OF LOW-MOLECULAR-WEIGHT CRYSTALLINS FROM CAMEL LENS (CAMELUS-DROMEDARIUS)

1. The use of an Ultrogel AcA 54 gel-filtration column separates camel lens cortex low molecular weight proteins into four peaks containing beta(s)-, GAMMA1-, GAMMA2- and GAMMA3-crystallins. 2. The molecular we ight of beta(s)-crystallin corresponded to 29 kDa on SDS PAGE and show ed three major bands between pH 5.85 and 8.45 on isoelectric focusing in addition, as compared to GAMMA-crystallins it has a lower degree of homology in amino acid composition, a low sulfhydryl content and a bl ocked N-terminal amino acid. 3. GAMMA1-, GAMMA2- and GAMMA3-crystallin s appeared homogenous on SDS PAGE and their molecular weights were rec orded as 23, 22 and 21 kDa. The isoelectric points of the GAMMA-crysta llin fractions ranged from pH 6.55 to 8.60 and they were found to have an unmodified glycine at the N-terminal end. 4. The three camel GAMMA -crystallin fractions were similar in molecular weight, isoelectric po ints, amino acid composition, sulfhydryl concentration and N-terminal amino acid.