(1) The ti was substituted into the first derivative function of the three exponents to yield the kie.
(2) After injection of 125 000 KIE aprotinin the restoration of the metabolic status was significantly retarded.
(3) The exponential factor of the fastest component (k1) and the initial exchange rate constant (kie) of cultured fibroblasts decrease in magnitude in response to incubation in K+-deficient medium or in the presence of ouabain and increase in magnitude when the cells are incubated in a Ca++-deficient medium.
(4) Larger KIE's are observed in the presence of Mn2+ as opposed to Mg2+.
(5) The values of Ki and Kies (apparent dissociation constants for inhibitor from enzyme-inhibitor and enzyme-inhibitor-substrate complexes, respectively) for the interactions of ponalrestat with ALR1 and ALR2 has been calculated by non-linear fitting of kinetic data.
(6) The synthetic gamma-polyglutamates are up to 2 orders of magnitude more potent as inhibitors of TS; e.g., the tetraglutamate (glu4) has a Ki of 1.0 nM (Kies = 15 nM).
(7) The average tunneling distance is shown to decrease when heavier isotopes are substituted for the hydrogen or when the temperature is increased, leading to kinetic isotope effects (KIEs)--defined as the factor by which the reaction slows down when isotopically substituted substrates are used--that need be no larger than KIEs for nontunneling mechanisms.
(8) Aprotinin in large doses (80,000 KIE kg-1) before xylene application reduced the fall in Pi, whereas indomethacin had no effect.
(9) 7 animals received 50,000 or 20,000 KIE respectively of a proteinase inhibitor after bleeding and immediately before and one hour after the infusion of Dextran 60.
(10) A restriction map of the cyanelle DNA from a different isolate of Cyanophora paradoxa (Kies-strain) was established.
(11) When the kie is further diminished (in the presence of both ouabain and phloretin) to the range of the exponential factor of the slowest component (k3), the washout of 22Na+ is apparently monoexponential.
(12) Inhibition of isolated L1210 TS by ICI D1694 is mixed noncompetitive (although tending toward competitive), with a Ki of 62 nM (Kies = 960 nM).
(13) The defects were filled with either pure fibrin glue or with glue containing aprotinin (3000 KIE), or with nothing (vacant).
(14) As the magnitude of the kie declines (in the presence of ouabain) to the level of the exponential factor of the middle component (k2), 22Na+ washout is adequately described by a two-exponential function.
(15) The values of Ki and Kies are 60 microM and 3 microM, respectively, so that inhibition tends towards uncompetitive.
(16) The values of Ki and Kies (dissociation constants for inhibitor from enzyme-inhibitor and enzyme-inhibitor-substrate complexes, respectively) for ICI 215918 with bovine kidney ALR1 and bovine lens ALR2S have been determined.
(17) ICI 215918 is a mixed noncompetitive inhibitor of ALR1 (Ki = 10 microM and Kies = 1.8 microM) when glucuronate is varied.
(18) Ponalrestat is a potent inhibitor (Ki = Kies = 7.7 nM) of ALR2 and follows a pure noncompetitive mechanism with respect to glucose.
(19) Therefore, the kie represents the equilibrium exchange rate constant for Na+ washout from an inhomogeneous cell-related space.
(20) No significant differences were detected when 1000 KIE aprotinin and 3 IU thrombin were used.