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.
Duhaiman
A S
AS
Department of Biochemistry, College of Science, King Saud University, Riyadh, Saudi Arabia.
Ajlan
A
A
Rabbani
N
N
al-Saleh
S
S
ElAmin
B
B
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002162:Camelus; D002850:Chromatography, Gel; D003459:Crystallins / Q000737:chemistry* / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D005998:Glycine / Q000032:analysis; D007526:Isoelectric Point; D007908:Lens, Crystalline / Q000737:chemistry*; D008970:Molecular Weight
D000596:Amino Acids; D003459:Crystallins; D005998:Glycine