Abstract
AbstractBovine serum albumin (BSA) was coupled to the reactive chloromethyl groups of poly(vinylbenzyl chloride) latex following the process both by the amount of BSA covalently bound and the chloride ion released. The primary bond formation is very insensitive to temperature with protein adsorption probably rate determining. Subsequent bond formation has an unusually high temperature coefficient and may depend on the deformability of the BSA molecule. On covalent bonding of ribonuclease 10% of the enzyme activity is retained.
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