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In: Archives of Biochemistry and Biophysics, Vol. 134, No. 1, 10.1969, p. 253-255.
Research output: Contribution to journal › Article › peer-review
TY - JOUR
T1 - Spectrophotometric and kinetic evidence for the existence of at least two salt-dependent conformations of α-chymotrypsin at pH values near neutrality
AU - Royer, G.
AU - Cuppett, C. C.
AU - Williams, E.
AU - Resnick, H.
AU - Canady, W. J.
N1 - Funding Information: K w and R, being the association constants for complex formation in pure water and in a solution of a given ionic strength, respectively. The yZ, 71, and “13 terms are activity coefficients at that given ionic strength for E, ES, and S, respectively. It was shown that 73 can be independently evaluated from the effect of salt on the solubility of the substrate. Equation 1 shows that the simplest explanation of the fact that the salting-out term is the predominant one is that the activity coefficients y1 and yt (of ES and E) are independent of ionic strength; added salt does not materially affect the state of ES or E. It will be seen that the data presented here support this formulation. The activity coefficient of E or ES refers primarily to the area of the active site since these data are kinetically derived. It was previously emphasized (1) that “the studies done so far do not attempt to deal with effects at very low ionic strengths, but rather with the gross effect of reasonably high concentrations of salts. All values quoted for pure water are extrapolated values obtained from plots of log I( against ionic strength.” 1 This work was supported 08122 of the National Institutes Grant GB 8143 of t,he National tion.
PY - 1969/10
Y1 - 1969/10
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U2 - 10.1016/0003-9861(69)90274-4
DO - 10.1016/0003-9861(69)90274-4
M3 - Article
C2 - 5345590
AN - SCOPUS:0014589797
SN - 0003-9861
VL - 134
SP - 253
EP - 255
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
IS - 1