Abstract
1.
1. The use of an Ultrogel AcA 54 gel-filtration column separates camel lens cortex low molecular weight proteins into four peaks containing
β
5-, Γ
1-, Γ
2-
and Γ
3-
crystallins
.
2.
2. The molecular weight of
β
5-
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 Γ-crystallins it has a lower degree of homology in amino acid composition, a low sulfhydryl content and a blocked
N-
terminal
amino acid.
3.
3.
Γ
1-, Γ
2-
and Γ
3-
crystallins
appeared homogenous on SDS-PAGE and their molecular weights were recorded as 23, 22 and 21 kDa. The isoelectric points of the Γ-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.
4. The three camel Γ-crystallin fractions were similar in molecular weight, isoelectric points, amino acid composition, sulfhydryl concentration and
N-
terminal
amino acid.