T. Yasuda et al., HUMAN SEMINAL DEOXYRIBONUCLEASE-I (DNASE-I) - PURIFICATION, ENZYMOLOGICAL AND IMMUNOLOGICAL CHARACTERIZATION AND ORIGIN, Clinica chimica acta, 218(1), 1993, pp. 5-16
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.