The study by Arthur Kamen, Felix Wróblewski, and John S. Ladue investigates the presence and activity of transaminase enzymes in human serum and blood. Transaminase enzymes catalyze the reversible transfer of the alpha amino nitrogen of an amino acid to an alpha-keto acid, producing a second amino acid and a second alpha-keto acid. The researchers used quantitative paper chromatography to measure the rate of glutamate formation, which is a measure of transaminase activity. The methods involved preparing solutions of aspartate, alanine, and alpha-keto glutarate in phosphate buffer and incubating them with serum or whole blood hemolysates. The incubation was followed by protein separation, chromatography, and color development to quantify glutamate. The results showed that transamination occurred in serum and hemolysates, with the rate of glutamate production proportional to the incubation time and the amount of serum. The study also found that pyridoxal phosphate and liver extract did not increase transaminase activity, suggesting that the enzyme was fully activated in the serum. The activity of glutamic oxalacetic and glutamic pyruvic transaminases was similar in normal human serum, but hemolysates had ten times more glutamic oxalacetic transaminase activity. The activity of these enzymes varied in patients with various diseases, particularly in those with acute myocardial infarction. The discussion highlights the sensitivity and simplicity of the paper chromatography method for measuring transaminase activity. The findings suggest that the serum transaminase enzymes have similar chemical characteristics to those found in animal tissues, and that the difference in activity between serum and hemolysates may be due to the rate of diffusion across cellular membranes or the source of the enzymes. The study concludes that transaminase activity is present in normal and diseased human blood, with significant variations in activity in patients with certain diseases.The study by Arthur Kamen, Felix Wróblewski, and John S. Ladue investigates the presence and activity of transaminase enzymes in human serum and blood. Transaminase enzymes catalyze the reversible transfer of the alpha amino nitrogen of an amino acid to an alpha-keto acid, producing a second amino acid and a second alpha-keto acid. The researchers used quantitative paper chromatography to measure the rate of glutamate formation, which is a measure of transaminase activity. The methods involved preparing solutions of aspartate, alanine, and alpha-keto glutarate in phosphate buffer and incubating them with serum or whole blood hemolysates. The incubation was followed by protein separation, chromatography, and color development to quantify glutamate. The results showed that transamination occurred in serum and hemolysates, with the rate of glutamate production proportional to the incubation time and the amount of serum. The study also found that pyridoxal phosphate and liver extract did not increase transaminase activity, suggesting that the enzyme was fully activated in the serum. The activity of glutamic oxalacetic and glutamic pyruvic transaminases was similar in normal human serum, but hemolysates had ten times more glutamic oxalacetic transaminase activity. The activity of these enzymes varied in patients with various diseases, particularly in those with acute myocardial infarction. The discussion highlights the sensitivity and simplicity of the paper chromatography method for measuring transaminase activity. The findings suggest that the serum transaminase enzymes have similar chemical characteristics to those found in animal tissues, and that the difference in activity between serum and hemolysates may be due to the rate of diffusion across cellular membranes or the source of the enzymes. The study concludes that transaminase activity is present in normal and diseased human blood, with significant variations in activity in patients with certain diseases.