Abstract
Human saliva contains enzymic activity which hydrolyzes α-n-benzoyl-l-arginine ethyl ester (BAEE) and which is inhibited by soybean trypsin inhibitor. The level of this activity in 20 patients with cystic fibrosis was 0.22±0.22 μmoles of BAEE hydrolyzed per hour per milligram of protein and in 19 control subjects 1.65±0.66. Twenty parents of patients with cystic fibrosis had levels corresponding to 1.05±0.51; 15 siblings had levels corresponding to 1.26±0.89 μmoles of BAEE hydrolyzed per hour per milligram of protein. Despite the fact that significant differences in trypsin-like activity could be demonstrated among patients, parents, and control subjects, the heterozygote could not be detected in all cases. Human saliva contains enzymic activity which hydrolyzes α-n-benzoyl-l-arginine ethyl ester (BAEE) and which is inhibited by soybean trypsin inhibitor. The level of this activity in 20 patients with cystic fibrosis was 0.22±0.22 μmoles of BAEE hydrolyzed per hour per milligram of protein and in 19 control subjects 1.65±0.66. Twenty parents of patients with cystic fibrosis had levels corresponding to 1.05±0.51; 15 siblings had levels corresponding to 1.26±0.89 μmoles of BAEE hydrolyzed per hour per milligram of protein. Despite the fact that significant differences in trypsin-like activity could be demonstrated among patients, parents, and control subjects, the heterozygote could not be detected in all cases.
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