By C. L. Tsou
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Copyright 1989. pK* +0 K m + [S] + *'. [S] 0 η K* + [S] Κ Ί ί Λ Δ ) Alternatively, subtracting equation 3 from equation 9 gives [PJcalc ~~ [Plobs ~ (A[Y] -f β) 2 6 [ 1 (13) ) f where [ P ] and [ P ] a r e t h e product c o n c e n t r a t i o n s a s calculated from equation 9 a n d the value actually o b s e r v e d at time t. 2). T h e value of Β gives the microscopic rate constant, / c _ , directly. T h e value of k c a n b e obtained by suitable plots of A against [S] a s before. F u r t h e r m o r e a plot of 1/A against [Y] results in a straight line parallel to t h e abscissa, showing that n o complex is formed prior to t h e inactivation step [10,13].
Since this crystal form diffracts m u c h better than the C crystal form and contains only o n e molecule in the a s y m m e t r i c unit, it is m o r e a d v a n t a g e o u s to further refine the structure in this form. 8 Ä data set has already b e e n collected. 2 4 2 2 4 2 sym 1 1 2 2 B. 2 is the stereo pair of the trichosanthin molecule. This is a p r o j e c t i o n of o n e molecule along the b-axis in the C form. 3 is its schematic drawing. T h e whole structure can be divided into t w o d o m a i n s with 167 residues in the N-terminal domain and 67 residues in the C-terminal domain.
W. Chi, Shanghai Institute of Biochemistry, for providing the mungbean trypsin inhibitor. References 1. 2. 3. 4. S. Maroux and P. Desnuelle, Biochim. Biophys. Acta 181, 59 (1969). D. D. Schroeder and E. Shaw, J. Biol. Chem. 243, 2943 (1968). R. L. Smith and E. Shaw, J. Biol. Chem. 244, 4704 (1969). B. Ru, J. Du, Y. Zeng, L. Chen, Y. Ni, G. Tan, and L. Zhang, Sei. Sin. (Engl. ) 23, 1453 (1980). 5. P. J. van Melle, S. H. Lewis, E. G. Samsa, and R. J. Westfall, Enzymologia 26, 133 (1963). 6. V. Kasche, Biochem, Biophys.