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- W2061426515 abstract "Two principal methods were described for the purification of the nonspecific hyaluronidase inhibitor in blood. The first, which gave a purification of 60 times, involved precipitation of the inhibitor by protamine sulfate and selective extraction with acetate buffer (pH 5.2). The second, which gave a purification of 130 times, depended on initial precipitation at pH 5.4, followed by ethanol fractionation. With increasing purification, an increase in concentration of metachromatic material was found, suggesting that the inhibitor contains an acid polysaccharide, possibly heparin. Eighty-five per cent of the material in preparations of purified inhibitor in solution of 0.1 ionic strength and pH 8.6 (veronal buffer) migrated electrophoretically as a single component with a mobility of approximately 6.6×10−5 cm.2/sec./v. The remaining material migrated at a slightly slower rate. The final purified inhibitor extract contained small amounts of prothrombin, thrombin, and caeruloplasmin. The former two were shown to have no effect on hyaluronidase inhibitor activity. A lack of parallelism between caeruloplasmin concentration, as determined by its blue color, and inhibitor activity has been demonstrated, but present evidence does not justify dismissal of the possibility that this substance is in some way related to inhibitor activity." @default.
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- W2061426515 date "1952-02-01" @default.
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- W2061426515 title "Mucolytic enzyme systems. XVII. Purification of the nonspecific hyaluronidase inhibitor in human blood" @default.
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- W2061426515 doi "https://doi.org/10.1016/s0003-9861(52)80008-6" @default.
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