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. 1973 Nov;136(3):721–729. doi: 10.1042/bj1360721

Identity of `acid' β-glucosidase and glucocerebrosidase in human spleen

Mae Wan Ho 1
PMCID: PMC1166008  PMID: 4780697

Abstract

1. Glucocerebrosidase, in association with a membrane-bound `acid' β-glucosidase, was separated from a soluble `neutral' β-glucosidase that had no activity towards glucocerebroside as substrate. 2. Glucocerebrosidase, as well as `acid' β-glucosidase activity depended upon the association of factor P (a heat-stable, soluble, acidic glycoprotein) with factor C (a heat-labile membrane-bound protein). 3. Factor C was solubilized under certain conditions. 4. Solubilized factor C, as well as membrane-bound factor C, could be alternatively stimulated by sodium taurocholate to give both glucocerebrosidase and `acid' β-glucosidase activities. 5. Membrane-bound factor C reacted optimally with factor P whereas solubilized factor C was preferentially stimulated by taurocholate. 6. Factor P-dependent glucocerebrosidase activity differed in kinetic properties from the taurocholate-stimulated enzyme activity. 7. The results are discussed in the light of (a) identity of glucocerebrosidase and `acid' β-glucosidase, (b) application in clinical diagnosis, (c) physiological significance of the enzyme system, and (d) polygenic inheritance in adult Gaucher's disease.

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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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