Based on indirect evidence it has been suggested that the liquefaction of human seminal plasma involves fibrinolytic and proteolytic enzymes and that the coagulum is formed by proteins. In this preliminary investigation evidence is presented for the involvement of seminal plasma sialyltransferase in liquefaction which suggests that the coagulum may be composed of glycoproteins. It is proposed that the glycoproteins form a polymer by the chelation of divalent metal ions via the carboxylic acid moieties of the sialic acid groups of the glycoproteins. The glycoprotein polymer may then be dismantled by the reduction of the meal ions by the oxidation of L-ascorbic acid, possibly allowing enzymes to complete the liquefaction process. A total of 100 semen samples from 30 male subjects whose semen profiles were considered "normal" by an independent assessor, were examined for the following: (i) liquefaction time of the seminal plasma; (ii) seminal plasma sialyltransferase activity; (iii) spermatozoal motility, defined as directional or nondirectional; (iv) spermatozoal count, and (v) seminal plasma content of free L-ascorbic acid, dehydroascorbic acid and glutathione. Linear regression analysis showed a significant correlation between sialyltransferase activity and the liquefaction time for seminal plasma. Similarly, multilinear regression analysis of the data showed that as the seminal plasma levels of L-ascorbic acid, total dehydroascorbic acid and glutathione increase, there is a decrease in spermatozoal motility and a decrease in the liquefaction time of the seminal plasma. The possible metabolic relationship of seminal plasma L-ascorbic acid and glutathione is discussed and a metabolic pathway is suggested.