Modification of amino groups in porcine pancreatic elastase with polyethylene glycol in relation to binding ability towards anti-serum and to enzymic activity |
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Authors: | A Koide S Kobayashi |
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Institution: | Eisai Tsukuba Research Laboratories, Eisai Co. Ltd. 1-3 Tokodai 5-chome Toyosato-machi Tsukuba-gun, Ibaragi 300-26 Japan |
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Abstract: | Porcine pancreatic elastase was modified by activated polyethylene glycol (2-0-methoxy-polyethyleneglycol-4, 6-dichloro-s-triazine) with molecular weight of 5000. The modification of elastase in which three amino groups out of the total four amino groups in the molecular gave rise to a complete loss of the binding ability towards anti-elastase serum from rabbit. The modified enzyme showed 35% of the original enzymic activity towards succinyl-L-alanyl-L-alanyl-L-alanine-p-nitroanilide and 17% towards casein. The heat-denatured collagen was also digested by the modified elastase, but the enzymic activity towards the elastin substrate was completely lost. The inhibition of the modified elastase activity by alpha 2-macroglobulin was found to be lesser than that of non-modified elastase. |
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