Studies on Protein Contents and Enzyme Activities of Human Seminal Plasma

On the basis of the semen analysis in 6G subjects, they were divided into six different groups: Group I .consisted of IG normal subjects with sperm counts of over 40x IOH/ml and motility of over 40 percent, 'Group II, 7 subjects with norn::al sperm counts but motility of under 40 percent, Group III, 1" oligospermic patients with under 40x 10'/ml, Group IV, 1/1 aaoospermic patients, Group V, 10 patients with vasectomy and Group VI, 4 abnormal patients with 2 hypoplastic testis, 1 klinefelter's syndrome and testis tumor. After separating sperm frem seminal plasma by ·centrifugation, the protein contents and the activities ·of hyaluronidase, p-K-acetylglucGsaminidase, ,S-glucuronidase, ar ylsulfatase. acrosin and azocoll proteinase were measured in the seminal plasma. Yasectornized group has 30 percent less of total protein than normal group. For the comparison of enzyme activities of seminal plasma, it could be assumed that the enzymes in seminal plasma were not contaminated with enzymes of spermatozoa by testing the enzymes of the seminal plasma from the vasectomized and az oosperrnic groups. I t had been reported that hyaluronidase was only released frem spermatozoa, however, the result obtained in this investigation showed that azoosperrnic and vasectomized group had high specific activities of hyaluronidase. The results indicated that hyahuonidasc was not only from the testis but also from the male accessory sexual glands. Oligospermic group (Group III) showed the lewest total activity of hyaluronidase among them. The specific activities of ~·N·acetylglucosaminidase was high in oligospermie group (Group Ill) and low in vasectomized group (Group V). These results were contradictory with the pattern of hyaluronidase activities. This indicated that the spermatozoa which were stayed in epididymis would increase the activity of this enzyme. The specific activity of ~·glucuronidase was low in oligospermic and vasectomized groups. Group VI including testis tumor had remarkably high arylsulfatase activity. Arylsulfatase, a typical lysosomal enzyme, has been known to be released unusually large amounts from certain tumor cells. Arylsulfatase was also released 'with high activities from azoosperrnic and vasectomized groups. This results indicated that this enzyme also released from the sources other than testis. Acrosin, a proteolytic enzyme locating In the sperm acrosome, was not found throughout all the samples of seminal plasma. The activities of azoco11 proteinase, a non-specific neutral proteinase VIas nearly identical in all the groups. This enzyme must have been released from the sources other than testis