Abstract
Entrapment in human α2-macroglobulin (α2M) of nonproteolytic enzymes was achieved with the help of trypsin covalently attached to the Sepharose matrix. While it was also possible to achieve entrapment by the exposure of the α2M: enzyme mixtures to soluble trypsin, use of the immobilized proteinase resulted in improved entrapment yields and also prevented the coentrapment of trypsin. Both soluble and immobilized trypsin transformed α2M to the electrophoretically fast form but the immobilized trypsin required relatively longer incubation to bring about the transformation. Horseradish peroxidase was entrapped in higher yield in α2M compared to the relatively high-molecular-weight invertase. α2M-entrapped peroxidase and invertase appeared highly accessible to their respective substrates, as evident from their relatively unaltered Km values. α2M-associated invertase, in spite of its large dimensions, failed to crossreact with the rabbit anti-invertase antiserum, indicating its physical entrapment rather than any other form of association.
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