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A previous communication from this laboratory1 as well as one from another3 described the separation of α2-macroglobulin from swine serum. The products from both laboratories contained, in addition to α2-macroglob-ulin, an additional macroglobulin contaminant with α2-globulln mobility. Due to their physicochemical similarity these macroglobulins are not resolved using conventional column procedures such as ion exchange chromatography and gel filtration. Subsequent experiments have shown that immunoelectro-phoretically pure swine α2-macroglobulln is present, in good yield (65%) in the breakthrough effluent of columns of Bio-Gel A-1.5m-Reactive Blue 2 while the contaminating macroglobulin is tightly bound. The production of highly purified swine α2-macroglobulin utilizing this observation is the subject of the present report. The product of the separation was found to be homogeneous when subjected to Immunoelectrophoresis, at a concentration of 14–16 mg/ml, and diffused against antiswlne whole serum antibody. The production of monospecific antibody, a more stringent test for homogeneity, resulted when the purified α2-macroglobulin was injected into rabbits. Physicochemical analyses on the purified product showed that swine and human α2-macro-globulins are true homologs.  相似文献   

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This symposium discusses J.-L. Dessalles's account of the evolution of language, which was presented in Why we Talk (OUP 2007).  相似文献   

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