Interactions of saccharides with concanavalin A. Relation between calcium ions and the binding of saccharides to concanavalin A.
作者： Curtis F. Brewer , Donald M. Marcus , Arthur P. Grollman , Himan Sternlicht
DOI: 10.1016/S0021-9258(19)42462-9
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摘要: Abstract Previous studies (Kalb, A. J., and Levitzki, (1968) Biochem. J. 109, 669; Shoham, M., Kalb, A.J., Pecht, I. (1973) Biochemistry 12, 1914) were interpreted as showing that transition metal calcium ions must be bound to concanavalin A before this lectin can bind sugars. In contrast, we find the addition of fails affect following properties manganese if metalloprotein is prepared in their presence: (a) ESR spectrum ion protein; (b) spin-lattice relaxation time solvent water protons measured presence (c) transverse times 13C carbons α-methyl-d-glucopyranoside (uniformly enriched with 14% 13C) These results indicate saccharide binding activity protein independent a (Mn2+) initially binds ions. The role appears accelerating rate formation final metal-protein complex observed by Barber Carver (Barber, B. H., Carver, P. Biol. Chem. 248, 3353).
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