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Discovery of a Homolog of Siderophilin in a Plant
Author(s) -
FEI YunBiao,
CAO PengXiu,
GAO SuQin,
WEI LingBo,
WANG Bin
Publication year - 2005
Publication title -
journal of integrative plant biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.734
H-Index - 83
eISSN - 1744-7909
pISSN - 1672-9072
DOI - 10.1111/j.1744-7909.2005.00159.x
Subject(s) - lactoferrin , size exclusion chromatography , biochemistry , transferrin , polyacrylamide gel electrophoresis , chemistry , gel electrophoresis , affinity chromatography , homology (biology) , sodium dodecyl sulfate , chromatography , amino acid , biology , enzyme
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‐Cellu‐lose‐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. (Managing editor: Wei WANG)