PubMed · 6994622
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N Colman, V Herbert. 1980. Folate-binding proteins.. https://doi.org/10.1146/annurev.me.31.020180.002245
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A multidisciplinary team of researchers at the University of Ottawa has expressed a human blood protein, granulocyte-macrophage colony stimulating factor, in tobacco seeds as part of a series of experiments whose ultimate goal is to express human blood proteins in cereal crops. Success in these experiments may lead to the development of a new, relatively inexpensive and ready supply of these proteins from a biologic source that is generally recognized as safe. The team is also studying the possibility of expressing in seeds proteins that may be used as vaccines against infectious diseases.
Electrophoresis of serum proteins is one of the traditional applications of zone electrophoresis. Whereas electrophoresis in supporting media uses usually 5,5'-diethylbarbiturate at pH 8.6 as the buffer, in capillary zone electrophoresis with on-line UV detection, this electrolyte is of little use because of its high UV absorbance. For that reason, a number of operational electrolytes differing in composition were tested for use in capillary electrophoresis of serum proteins. The influence of the pK(A) of co-ions and counter ions and the concentration of the operational electrolyte was examined. If 0.1 M methylglucamine-0.1 M epsilon-aminocaproic acid or 0.1 M methylglucamine, -0.1 M gamma-aminobutyric acid is used as the operational electrolyte, capillary electrophoresis separates serum proteins into more than ten zones.
The susceptibility of vitronectin (Vn) purified from human plasma to digestion by matrix metalloproteinases (MMPs) was examined. MMP-2, -3, -7 and -9 except for MMP-1 degraded Vn into multiple fragments. MMP-7 showed the highest activity to the substrate among these MMPs, digesting 8-, 30- and 44-fold more preferentially than MMP-2, -3, and -9, respectively. These data suggest that MMP-2, -3, -7 and -9 may be responsible for the pathological degradation and/or normal turnover of Vn.