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    Biochim Biophys Acta. 1993 Oct 6;1202(2):277-80.

    Disulfide bridge structure of the heat-stable sweet protein mabinlin II.

    Nirasawa S, Liu X, Nishino T, Kurihara Y.

    Source

    Department of Chemistry, Faculty of Education, Yokohama National University, Japan.

    Abstract

    The heat-stable sweet protein mabinlin was composed of a A-chain of 33 amino-acid residues and a B-chain of 72 amino-acid residues (Liu, X., Maeda, S., Hu, Z., Aiuchi, T., Nakaya, K. and Kurihara, Y. (1993) Eur. J. Biochem. 211, 281-287). A-chain and B-chain contain two and six cysteine residues, respectively. The formation of two interchain disulfide bridges at Cys(A5)-Cys(B21) and Cys(A18)-Cys(B10), and two intrachain disulfide bridges at Cys(B11)-Cys(B59) and Cys(B23)-Cys(B67) were determined by amino-acid sequencing and composition analysis of cystine-containing peptides isolated by HPLC. Cleavage of the disulfide bridges with dithiothreitol results in complete loss of the sweet activity of mabinlin II. It was suggested that the structure fixed by four disulfide bridges contributes to heat stability of mabinlin II.

    PMID:
    8399391
    [PubMed - indexed for MEDLINE]

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