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Trypsin transition temperature

A second set of data are temperature jump studies of trypsin denaturation near pH 2 made by Pohl (59), Fig. 20. Temperature changes near the transition temperature can, of o>urse, change the degree of folding markedly in Pohl s setup rather large jumps can be m e, but these are relatively slow, the maximum observable rate is only 0.5sec ... [Pg.269]


See other pages where Trypsin transition temperature is mentioned: [Pg.727]    [Pg.165]    [Pg.68]    [Pg.87]    [Pg.390]    [Pg.470]    [Pg.396]    [Pg.100]    [Pg.121]    [Pg.1260]    [Pg.673]    [Pg.75]    [Pg.393]    [Pg.517]    [Pg.382]    [Pg.342]    [Pg.48]    [Pg.123]    [Pg.140]    [Pg.54]   
See also in sourсe #XX -- [ Pg.727 ]




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