Early proteolytic cleavage with loss of a C-terminal fragment underlies altered processing of the beta-galactosidase precursor in galactosialidosis.

@article{OkamuraOho1996EarlyPC,
  title={Early proteolytic cleavage with loss of a C-terminal fragment underlies altered processing of the beta-galactosidase precursor in galactosialidosis.},
  author={Y Okamura-Oho and Shaobo Zhang and W L Hilson and Aleksander Hinek and John William Callahan},
  journal={The Biochemical journal},
  year={1996},
  volume={313 ( Pt 3)},
  pages={787-94}
}
Processing of human beta-galactosidase (beta-GAL) was studied in permanently transfected Chinese hamster ovary (CHO) cells and compared with that in normal cells and in cells from subjects with GM1-gangliosidosis, galactosialidosis and I-cell disease. Biosynthesis of beta-GAL in CHO cells results in the synthesis of an 88 kDa glycosylated and phosphorylated monomer precursor which is enzymically active and is secreted into the medium. Post-translational processing begins at the C-terminal end… CONTINUE READING

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