The state of tryptophan-containing sites of human, bovine and rabbit plasminogens with changing solution pHs.
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.
Nikandrov
V N
VN
Laboratory of Biochemistry, Byelorussian Research Institute of Epidemiology and Microbiology, Minsk.
Vorobyova
G V
GV
Demidchik
N V
NV
D000818:Animals; D002417:Cattle; D006801:Humans; D006863:Hydrogen-Ion Concentration; D010958:Plasminogen / Q000737:chemistry*; D011817:Rabbits; D012997:Solvents; D013050:Spectrometry, Fluorescence; D014364:Tryptophan / Q000032:analysis / Q000737:chemistry*
D012997:Solvents; D014364:Tryptophan; D010958:Plasminogen