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. 1978 Dec 1;175(3):1013–1022. doi: 10.1042/bj1751013

Characterization of the mutant α-mannosidase in bovine mannosidosis

Lynda J Burditt 1,2, Nigel C Phillips 1,2,*, Donald Robinson 1,2, Bryan G Winchester 1,2, Neil S Van-De-Water 1,2, Robert D Jolly 1,2
PMCID: PMC1186164  PMID: 743225

Abstract

Residual acidic α-mannosidase, varying in amount up to approx. 15% of normal values, can be measured in various organs of a calf with mannosidosis. The highest specific activity and relative proportion of residual activity were found in the liver. Chromatography on DEAE-cellulose showed that the residual activity was associated with two components, which were eluted at comparable positions with those found in normal tissues. The residual activity had a lower thermal stability and a higher Km value for a synthetic substrate than did the normal enzyme. No differences in molecular weight or electrophoretic mobility between normal acidic α-mannosidase and the residual activity were observed by gel filtration and electrophoresis on cellulose acetate respectively. The isoelectric focusing profiles for the α-mannosidase in the normal and pathological livers were very similar. It is suggested that a mutant enzyme, resulting from a mutation in a structural gene, accounts for the residual acidic α-mannosidase in mannosidosis. The mutant enzyme, which cross-reacts with antiserum raised against normal bovine acidic α-mannosidase, is present at a decreased concentration compared with the normal enzyme. There is a correlation between the concentrations of residual activity and cross-reacting material in mannosidosis. α-Mannosidase with a pH optimum of 5.75 and which is activated by Zn2+ was also detected in the liver of the calf with mannosidosis. However, it is probably not a product of the defective gene because addition of Zn2+ indicated that it was also present in normal tissues.

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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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