The state of tryptophan-containing sites is proved to be stable by intrinsic tryptophan fluorescence with pH 5-8, 7-9, and 6-9 in human, rabbit and bovine plasminogen molecules, respectively. With pH < 5.0 tryptophan-containing sites of human zymogen (in contrast to rabbit and bovine ones) undergo conformational transitions. With the shift of solution pH from 9 to 12 tryptophan-containing sites of human and rabbit plasminogens are partially disorganized, while tryptophanyls become more available for solvent. Tryptophan-containing sites of bovine plasminogen molecules are less mobile in structure during changes of solution pH.
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