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. 1981 Feb 1;193(2):651–654. doi: 10.1042/bj1930651

Deficient phosphorylation of mannose residues of mannan in fibroblasts of patients with mucolipidoses II and III.

Y Ben-Yoseph, L C Hahn, C L DeFranco, H L Nadler
PMCID: PMC1162646  PMID: 7305949

Abstract

Incorporation of 32P from [gamma 32P]ATP into mannan could not be detected in homogenates of cultivated skin fibroblasts from patients with mucolipidosis II, and accounted for only up to 10% of normal control activity in cell lysates from patients with mucolipidosis III. Parents of patients with mucolipidosis II demonstrated 60-70% of normal control activity. On high-voltage electrophoresis, the hydrolysed mannan from reactions performed with normal cells, over the pH range 5.5-7.5, yielded a radioactive band migrating with the same mobility as mannose 6-phosphate, whereas no such product could be demonstrated in fibroblasts of patients with mucolipidosis II.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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