Reference: Mrsa V, et al. (1987) Role of glycosylation in secretion of yeast acid phosphatase. FEBS Lett 217(2):174-9

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Abstract


The minimal glycosylation requirement for acid phosphatase secretion and activity was investigated using tunicamycin, an inhibitor of protein glycosylation, and a yeast mutant defective in the synthesis of oligosaccharide outer chains. The results obtained show that outer chain addition is not essential for secretion of active enzyme and that only 4 core chains, out of 8 normally attached to a protein subunit, are sufficient for enzyme transport to the periplasmic space. Enzyme forms with less than 4 chains were retained in membranes of endoplasmic reticulum. Secreted underglycosylated enzyme forms are partially or completely inactive.

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Journal Article | Research Support, Non-U.S. Gov't
Authors
Mrsa V, Barbarić S, Ries B, Mildner P
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