Increased cleavage of the c-terminal serine from alpha-A crystallin present in the high molecular weight aggregate fraction from human and bovine lenses

1999 ◽  
Vol 19 (5) ◽  
pp. 450-455 ◽  
Author(s):  
Larry Takemoto
1980 ◽  
Vol 190 (2) ◽  
pp. 229-237 ◽  
Author(s):  
J G Heathcote ◽  
A J Bailey ◽  
M E Grant

1. Intact rat lenses in tissue culture synthesize hydroxy[3H]proline-containing polypeptides of apparent mol.wt. approx. 180000, which become assembled into aggregates of higher molecular weight with time. 2. Both the 180000-mol.wt. species and the aggregates are components of the deoxycholate-insoluble base-membrane matrix. 3. Formation of the high-molecular-weight aggregate is accompanied by the biosynthesis of the reducible hydroxylysine-derived cross-link hydroxylysino-5-oxo-norleucine. 4. Hydroxylysino-5-oxonorleucine and dehydrohydroxylysinonorleucine are the major reducible cross-links present in intact foetal and 1-month-old calf lens capsules.


1983 ◽  
Vol 50 (2) ◽  
pp. 417-425 ◽  
Author(s):  
David Sklan

1. A fluorescent high-molecular weight lipid–protein aggregate was isolated from the cytosol of chick intestinal mucosa or liver by gel filtration on columns of Sepharose 4B or 6B.2. This aggregate exhibited carotene-cleavage activity.3. On incubation of this aggregate, dissociation occurred and low-molecular weight fractions containing Cu and Zn and exhibiting carotene-cleavage activity were found. This fraction appeared on sodium dodecyl sulphate polyacrylamide electrophoresis to have a molecular weight of 7000–11000 and resembled the previously described Cu chelatins in amino acid composition.4. Carotene cleavage may be effected by a copper–zinc metalloprotein of low-molecular weight, associated in intestinal cytosol with a lipid–protein aggregate.


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