[Study on soluble proteins in human fetal lens].
Soluble proteins from corter of human fetal clear lenses were separated by column chromatography with Sepharyl S-300 (superfine) and determined by disc-PAGE and SDS-PAGE. The results documented from 18W, 21W (2 cases) and 24W fetal lenses suggested that a negative correlation tended to be presented between the age of fetus and fraction of alpha, beta 1 crystallins (r = -0.9542; r = -0.9674) and a positive correlation between the age of fetus and fraction of beta 2, gamma crystallins (r = 0.9666; r = 0.9970). There was no change in the alpha, beta 1, beta 2 crystallins on disc-PAGE. Among the fetuses of different ages, the blurred band of gamma crystallin seen in 18W and 21W fetal lenses was thickened in the 24W fetal lens. The SDS-PAGE showed that there was no significant difference among the polypeptides in each of alpha, beta 1, beta 2, gamma crystallins in the studied fetal lenses of different age groups. It is presumed that the normal lens is proportionally composed of four fractions of crystallin. This is hypothetically contributed to the maintenance of normal structure of the lens, why the proper proportion of four fractions of crystallins is depended either on proteins synthesis or on protein molecular assembly is not yet clear.
Cao
X
X
Zhongshan Ophthalmic Center, Sun Yat-sen University of Medical Sciences, Guangzhou, China.
Li
S
S
Pan
S
S
Liang
S
S
Wu
K
K
Huang
Q
Q
D002850:Chromatography, Gel; D003459:Crystallins / Q000145:classification / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D005333:Fetus; D006801:Humans; D007908:Lens, Crystalline / Q000737:chemistry* / Q000196:embryology
D003459:Crystallins