Properties of purified salivary ribonuclease, and salivary ribonuclease levels in children with cystic fibrosis and in heterozygous carriers.

Alkaline acid- and thermo-stable ribonuclease was isolated from human saliva of healthy subjects, children with cystic fibrosis, and from parents of the latter. The enzyme was purified about 180-200 times, and its ionic requirements, and specificity towards various substrates, characterized and compared with those for human pancreatic ribonuclease. The level of acid- and thermo-stable ribonuclease activity was five times higher in terms of enzyme level per ml saliva, and three times higher in terms of salivary protein, for 62% of children with cystic fibrosis, and for 73% of carrier subjects, relative to co-nrol groups. Assay of the level of this ribonuclease activity appears to be a promising diagnostic tool for detection of heterozygote carriers.