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-, gamma 1-, gamma 2- and gamma 3-crystallins. 2. The molecular weight of beta s-crystallin corresponded to 29 kDa on SDS-PAGE and showed 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 blocked N-terminal amino acid. 3. gamma 1-, gamma 2- and gamma 3-crystallins appeared homogenous on SDS-PAGE and their molecular weights were recorded as 23, 22 and 21 kDa. The isoelectric points of the gamma-crystallin 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 points, amino acid composition, sulfhydryl concentration and N-terminal amino acid.