HUMAN SEMINAL DEOXYRIBONUCLEASE-I (DNASE-I) - PURIFICATION, ENZYMOLOGICAL AND IMMUNOLOGICAL CHARACTERIZATION AND ORIGIN

Deoxyribonuclease I (DNase I) was purified from the semen of a 38-year -old male and then characterized. The catalytic properties of the puri fied enzyme closely resembled those of DNase I purified from the urine of this individual and the following other similarities were observed : molecular masses, iodoacetic acid inactivation kinetics, desialylate d isoenzyme patterns. However, the behavior of the purified enzymes de termined on several different lectin-affinity chromatography columns d iffered, which suggests that organ-specific glycosylation of DNase I o ccurs. Multiple forms of the purified seminal DNase I were demonstrate d, each of which had a different pI value separated by isoelectric foc using, which is compatible with the reported existence of genetic poly morphism of seminal DNase I (Sawazaki et al., Forensic Sci Int 1992;57 :39-44). Furthermore, enzymological and immunological comparisons of p urified seminal and urinary and partially purified prostatic DNases I indicated that the prostate may be one of seminal enzyme source tissue s.