PROTEOLYTIC BREAKDOWN OF HUMAN INTER-ALPHA-TRYPSIN INHIBITOR BY PLASMIN

  • 1 January 1977
    • journal article
    • research article
    • Vol. 25, 31-34
Abstract
Inter-.alpha.-trypsin inhibitor was isolated from human plasma and submitted to proteolytic degradation by plasmin. A split product of low MW (18,000 daltons) is obtained by gel filtration or solubilization in perchloric acid. This fragment reacts with an anti-inter-.alpha.-trypsin inhibitor immune serum and migrates as .beta.1-globulins. Its specific activity against trypsin (after absorption of residual plasmin on sepharose-lysine) was estimated to be 900 mUl[amount which inhibits 1 milliunit of trypsin]/mg. One molecule of the fragment can inhibit 1 molecule of trypsin. Complexes formed with trypsin can be dissociated by urea or sodium dodecyl sulfate. This fragment is similar to the small MW inhibitors obtained directly by solubilization in perchloric acid from serum, urine and bronchial secretions.

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