Abstract
1. Inhibition of ox liver glutamate dehydrogenase with N-(N′-acetyl-4[35S]-sulphamoylphenyl)maleimide (ASPM) is more specific at pH7·3 than at pH6·9. At pH7·3 inhibition accompanies the incorporation at 1 mole of ASPM residues into about 53000g. of protein. 2. Digestion of the modified protein with chymotrypsin and trypsin yields a unique radioactive peptide. 3. Acid hydrolysis of 1 mole of this peptide yields 1 mole of N∈-succin-2-yl-lysine. The ∈-amino group of a lysyl residue is thus the site of modification of the protein. 4. The sequence containing the modified lysyl residue is: [Formula: see text] where Asx respresents either aspartic acid or asparagine.
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