|
|
||||||||
1 Department of Ophthalmology, College of Physicians & Surgeons, Columbia University, New York, N. Y. 10032
Newly synthesized
-crystallin (NS
) appears relatively homogeneous with an apparent average molecular weight (MW) of 7.4 x 105 ± 3 per cent. It is composed primarily of polypeptide chains A2 and B2. Only trace amounts of B1 and small amounts of A1 can be detected. Both A1 and B1 are produced rapidly through post-translational events. Low molecular weight
-crystallin (LMW
) arises from NS
and is composed of 4 polypeptide chains, B1, B2, A1, and A2, with B1 representing approximately 11 per cent of the total polypeptide population and A1 approximately 24 per cent. Little change can be detected in the LMW
polypeptide composition isolated from three-month-old calf lens cortex or nucleus or from two-year-old steer lens nucleus. High molecular weight
-crystallin (HMW
) from calf lens periphery has a polypeptide-chain profile similar to that of LMW
. However, HMW
from calf lens nucleus shows changes in its polypeptide profile which become more pronounced in steer nucleus HMW
. Of particular interest is the appearance of two components with MW's of 17,000 and 13,000 and a splitting of the A1 urea polyacrylamide electrophoresis band. HMW
from steer nucleus was also found to contain a substantial amount of atypical A-chains with masked SH groups. It is suggested that age-dependent changes in the polypeptide-chain composition of
-crystallin affect both its size and physical homogeneity.
Note:
Postdoctoral trainee of the National Eye Institute.
Special Fellow of the National Eye Institute.
Key Words: alpha-crystallin polypeptide chains A1, A2, B1, and B2 newly synthesized low molecular weight high molecular weight
Submitted on August 6, 1973
Accepted on September 26, 1973
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |