The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
Purification and Characterization of Two Lectins from Aloe arborescens Mill
Ikuo SUZUKIHiroko SAITOShigeki INOUEShunsuke MIGITATaijo TAKAHASHI
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1979 年 85 巻 1 号 p. 163-171

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Two lectins have been isolated from leaves of Aloe arborescens Mill by salt precipitation, pH-dependent fractionation and gel filtration. One lectin (P-2) has a molecular weight of approximately 18, 000, consists of two subunits (αβ) and contains more than 18% by weight of neutral carbohydrate. The smaller subunit (α) has a molecular weight of approximately 7, 500 and the larger subunit (β) a molecular weight of approximately 10, 500. The other lectin (S-1) has a molecular weight of approximately 24, 000, consists of two subunits (γ2) with a molecular weight of approximately 12, 000 and contains more than 50% by weight of neutral carbohydrate. An interesting feature of the amino acid compositions of these lectins is the high proportion of acidic amino acids, such as aspartic acid and glutamic acid, and the low proportion of methionine and histidine.
S-1 has a strong hemagglutinating activity. On the other hand, P-2 has not only hemag-glutinating activity but also mitogenic activity on lymphocytes, precipitate-forming reactivity with serum proteins, one of which is α2-macroglobulin, and complement C3 activating activity via the alternate pathway.
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© The Japanese Biochemical Society
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