The coagulation and liquefaction process of human semen was studied in some detail. It was found that contact of seminal vesicle fluid with the other accessory sex gland secretions or spermatozoa does not seem to be essential for the formation of the coagulum, and that heparin and sodium citrate do not affect coagulum formation, indicating a difference between the seminal coagulation process and that of the blood clot. Regarding the liquefaction process of the seminal coagulum, it was shown that 1) spermatozoa do not influence liquefaction; 2) that the seminal plasminogen activator, lysozyme, α‐amylase, pepsin, and neuramini dase are not the primary liquefying factors; 3) that the liquefying agent is present in the first portion of a split ejaculate, is heat labile, is partially destroyed by freezing at −20 C but is stable to lyophilization, is precipitable with (NH4)2SO4, is not affected by serum or EDTA, and is inhibited by rabbit bile but not by the seminal plasma proteinase inhibitors, the Kunitz pancreatic trypsin inhibitor, or epsilon‐aminocaproic acid (EACA). All of these prop erties are characteristics of the seminal en zyme, seminin. A partially purified preparation of this enzyme enhanced liquefaction, and two patients who had low seminin activity pos sessed poorly lysing coagula. These findings confirm that seminin is the agent primarily re sponsible for liquefaction of the seminal coagulum of man. The data further show that liquefaction of the seminal coagulum occurs by a different mechanism than that of the lysis of the blood clot.

hCG hormone is a naturally occurring, immune-modulating agent, which is highly expressed during pregnancy and causes improvements of some autoimmune diseases such as multiple sclerosis and Crohn's disease. Little is known about its immune-modulating effects. This study in MNCs of women who received hCG as preconditioning prior to IVF demonstrates that hCG increases anti-inflammatory IL-27 expression and reduces inflammatory IL-17 expression. In addition, we found increased IL-10 levels and elevated numbers of Tregs in peripheral blood of women after hCG application. Rejection of allogeneic skin grafts was delayed in female mice receiving hCG. We conclude that hCG may be useful for the induction of immune tolerance in solid organ transplantation.

Two plasminogen activators (1 and 2) were isolated from human seminal plasma by hiigh-speed centrifugation, Sephadex-gel filtration and ion-exchange chromatography. The activators were shown to be homogeneous by polyacrylamide-disc -gel electrophoresis at pH 8.3 and 4.5, and by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. The molecular weights of activators 1 and 2 were estimated as 69 000 and 74 000. Their amino acid compositions are very similar, both being high in aspartic acid, glutamic acid, serine, glycine and leucine, and low in methionine, tryptophan, tyrosine, isoleucine and histidine. Activators 1 and 2 each possess 16 cysteine residues. Both activators have isoelectric points of approx. 7.0, are stable over a wide pH range at temperatures up to 60 degrees C, but lose activity at higher temperatures, particularly under very basic or acidic conditions. They are not inhibited by EDTA, Mg2+ and Ca2+ at 10 mM concentrations, but their activity decreases on addition of 10 mM-cysteine or Fe2+ and 6-aminohexanoate or sera from pregnant women. The precipitin band formed between urokinase and its antiserum is continuous with the precipitin bands formed between the seminal plasminogen activators and the urokinase antiserum. Antisera to urokinase inhibit both the activity of urokinase and the seminal plasminogen activators.

No abstract

Summary. The concentrations of spermatozoa, fructose, IgG, IgA, albumin, lactoferrin, transferrin, secretory piece of IgA, \ g=b\ 1C/ \ g=b\ 1A\ x=r eq-\ globulin (C\m='\3-component of complement), ceruloplasmin and fibrinogen were evaluated in human split ejaculates and/or in whole human seminal plasma. The concentrations of spermatozoa, IgG, IgA, albumin and transferrin decreased from the first portion of the split ejaculate to the last, indicating that these proteins originate mostly from secretions other than the seminal vesicles. By contrast, the highest amounts of fructose and lactoferrin were present in the final portion of the split ejaculates, showing their seminal vesicle origin. No secretory piece, IgM, \ g=b\ 1C/ \ g=b\ 1A\ x=r eq-\ globulin, ceruloplasmin or fibrinogen could be detected in human semen. An unidentified antigen was found that has a relatively high molecular weight and shows \g=b\1-mobility on immunoelectrophoresis.