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The alpha-mannosidase from Canavalia ensiformis seeds: chemical and kinetic properties and action on animal lymphocytes.

Biological chemistry Hoppe-Seyler (1988-03-01)
W Einhoff, H Rüdiger
RÉSUMÉ

The alpha-mannosidase from Canavalia ensiformis was characterized with respect to molecular mass, glycoprotein nature, amino-acid composition, enzymic properties and action on animal cells. The enzyme is composed of two pairs of subunits (molecular mass 44 and 66 kDa) which form a tetramer (220 kDa). The larger subunit is glycosylated, the smaller one is not. Both subunits have similar amino-acid compositions. The larger subunit contains a surplus of alanine, aspartic acid/asparagine, histidine, phenylalanine and tyrosine, the smaller one a surplus of glutamic acid/glutamine, serine and threonine. The enzyme is subject to product inhibition by mannose. It stimulates the proliferation of B-lymphocytes from nude mice.

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Sigma-Aldrich
α-Mannosidase from Canavalia ensiformis (Jack bean), ammonium sulfate suspension, ≥15 units/mg protein (biuret)