Abstract
Rat liver Golgi stacks were extracted with Triton X-100 at neutral pH. After centrifugation the low speed pellet contained two medial-Golgi enzymes, N-acetylglucosaminyltransferase I and mannosidase II, but no enzymes or markers from other parts of the Golgi apparatus. Both were present in the same structures which appeared, by electron microscopy, to be small remnants of cisternal membranes. The enzymes could be removed by treatment with low salt, leaving behind a salt pellet, which we term the matrix. Removal of salt caused specific re-binding of both enzymes to the matrix, with an apparent dissociation constant of 3 nM for mannosidase II. Re-binding was abolished by pretreatment of intact Golgi stacks with proteinase K, suggesting that the matrix was present between the cisternae.
Dates
Type | When |
---|---|
Created | 21 years, 3 months ago (May 14, 2004, 8:22 p.m.) |
Deposited | 2 years, 1 month ago (July 22, 2023, 12:36 a.m.) |
Indexed | 4 months, 2 weeks ago (April 8, 2025, 9:58 p.m.) |
Issued | 31 years, 6 months ago (Feb. 15, 1994) |
Published | 31 years, 6 months ago (Feb. 15, 1994) |
Published Online | 31 years, 6 months ago (Feb. 15, 1994) |
Published Print | 31 years, 6 months ago (Feb. 15, 1994) |
@article{Slusarewicz_1994, title={Isolation of a matrix that binds medial Golgi enzymes}, volume={124}, ISSN={1540-8140}, url={http://dx.doi.org/10.1083/jcb.124.4.405}, DOI={10.1083/jcb.124.4.405}, number={4}, journal={The Journal of cell biology}, publisher={Rockefeller University Press}, author={Slusarewicz, P and Nilsson, T and Hui, N and Watson, R and Warren, G}, year={1994}, month=feb, pages={405–413} }