John T. Edsall

Learn More
Although the full evidence for this scheme is not yet available, it is clearly more general than the “classical” reaction scheme (see e.g. Edsall and Wyman (5)), which assumed that k13 = kal = 0. The constants klz and ks, are very large, k12 probably being of the order of 5 x lOlo ~hl se@, and kzl of the order of 107 see-1 (3). The absolute values of these(More)
A stop-flow kinetic study was performed on the carbon dioxide hydration activity of the human carbonic anhydrase B isoenzyme carboxymethylated at its histidine(200), and of the human C isoenzyme carboxyketoethylated at its histidine(63). The Michaelis-Menten parameters determined between pH 5.6 and 8.7 showed striking differences between the native and the(More)
The tyrosyl groups of reduced and carboxymethylated human serum albumin, in which all disulfide bonds are broken, ionize at lower pH than those of native albumin, in spite of the greater negative charge on the protein produced by the S-carboxy-methyl groups. The heat and entropy of ionization of these groups in the reduced albumin are also "normal," in(More)
The ultraviolet absorption of protein solutions at wave lengths greater than 2500 A is due chiefly to the aromatic side chains of tyrosine, phenylalanine, and tryptophan (1,2). When a protein is titrated with a.lkali, a ncm, stronger absorption band appears with a maximum at about 2930 A, because of the ionization of tyrosyl residues. This marked change in(More)
Three different methods are described for separating hemoglobins from carbonic anhydrases in hemolysates from human erythrocytes. The preferred method involves adsorption on diethylaminoethyl Sephadex at pH 8.7 followed by selective elution of the carbonic anhydrases. Carbonic anhydrases A, B, and C are subsequently separated from each other on(More)