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Oleosins stabilize oil bodies in seeds and other tissues and contain a unique hydrophobic domain which appears to be inserted into the oil matrix as an α-helical hairpin. The oleosin proteins may be exploited to stabilize emulsions while the ease of oil body preparation has led to the expression of bioactive proteins as oleosin fusions in molecular farming.
An M r 22 500 protein was purified from isolated oil bodies from sunflower cotyledons. N-terminal amino acid sequencing showed that this protein belonged to the 2S albumin group of storage proteins. A corresponding cDNA clone encoded a preproprotein, comprising two mature 2S albumin proteins one of which corresponded to the oil-body associated albumin. In contrast, the second albumin encoded...
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