J Integr Plant Biol. ›› 2005, Vol. 47 ›› Issue (12): 1409-1411.DOI: 10.1111/j.1744-7909.2005.00159.x

• Research Articles •     Next Articles

Discovery of a Homolog of Siderophilin in a Plant

Yun-Biao FEI, Peng-Xiu CAO, Su-Qin GAO, Ling-Bo WEI and Bin WANG   

Abstract: Members belonging to the siderophilin family are iron-binding and iron-transporting proteins, which includes transferrin and lactoferrin. They have only been found in animals previously. If siderophilin could be found in and isolated from a plant, its production and subsequent extensive application could be increased. The present study is the first to report the discovery of a homolog of siderophilin in a plant. In order to purify antifreeze proteins from Ammopiptanthus mongolicus (Maxim.) Cheng f., the authors processed the proteins from the leaves using techniques such as column chromatography using DEAE-Cellulose-52, gel filtration via Sephacryl S-100 HR medium, hydrophobic interaction chromatography, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Mass spectroscopy was performed on the three proteins purified and the sequence of one of the proteins (containing 32 amino acids) was found to have 97% homology with the corresponding part of one type of human lactoferrin. Moreover, one of the two peptides belongs to an iron-binding domain. So, it is possible that siderophilin also exists in plants and plays a role as an antibacterial and antifungal, among other actions.

Key words: antibacterial, iron-binding domain, lactoferrin, siderophilin, transferrin.

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