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• W2042569530 abstract "The amino-acid sequences of the subunits of the lectin BMA from seeds of Bowringia mildbraedii have been determined. The data indicate that the lectin consists of a precursor polypeptide of approx. 29 kDa that is cleaved almost completely into two fragments of approx. 13.3 kDa (α subunit) and approx. 11.9 kDa (β subunit), respectively. The β subunit represents the N-terminal half of precursor polypeptides and is disulphide-linked in a ββ dimer in the native (αβ)2 protein. BMA shows extensive amino-acid sequence homologies with known legume lectins. The site of post-translational proteolysis of the putative precursor occurs at a position similar to that identified in lectins obtained from other Sophoreae plants such as Sophora japonica and in Diocleae lectins such as Concanavalin A, but different from that of two chain lectins obtained from other tribes of the Papilionaceae." @default.
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• W2042569530 date "1993-09-01" @default.
• W2042569530 modified "2023-09-25" @default.
• W2042569530 title "Bowringia mildbraedii agglutinin: polypeptide composition, primary structure and homologies with other legume lectins" @default.
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• W2042569530 doi "https://doi.org/10.1016/0167-4838(93)90060-5" @default.
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