Binding of Lactose and Galactose to Native and lodinated Ricin D

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概要

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• The binding of lactose and galactose to native and iodinated ricin D was investigated by equilibrium dialysis and ultraviolet difference spectroscopy. The results provided direct evidence that native ricin D has two independent saccharide binding sites with different affinities, of which the high-affinity (HA-) binding site is able to bind with both lactose and galactose while the lowaffinity (LA-) binding site binds only with lactose. In contrast, the iodinated ricin D possesses only one binding site both for lactose and galactose with high affinity. By UV-difference spectroscopic analysis we found that there is one tyrosyl residue at or near the HA-binding site in ricin D which may be involvled in binding with saccharide. This tyrosyl residue was not iodinated in the presence of lactose but was iodinated in the absence of lactose and was perturbed by an addition of lactose even after iodination. From these results, it was inferred that the binding site abolished by the iodination is the LAbinding site and this may be due to the conformational alteration of the LA-binding site caused by the iodination of the tyrosyl residue(s) present near the LA-binding site.

• 社団法人 日本農芸化学会の論文

著者

• Funatsu Gunki

  Laboratory Of Biochemistry And ** Laboratory Of Protein Chemistry & Engineering Faculty Of Agric

• Shimoda Tadahisa

  Laboratory Of Biochemistry Faculty Of Agriculture Kyushu University

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