Changes in porcine sperm lactate dehydrogenase isoenzymes during sperm maturation.

The changes in sperm lactate dehydrogenase (LDH-lactate: NAD oxidoreductase, EC 1.1.1.27) activity and the relative occurrence of LDH isoenzymes during sperm maturation were studied using pubertal German improved Landrace boars. The LDH of spermatozoa liberated from the testis, caput epididymis, proximal and distal corpus epididymidis and cauda epididymidis was spectrophotometrically quantified while the LDH isoenzymes were separated on fine cellulose acetate membrane strips with the Sartorius Sartophor system. The LDH content of sperm dropped drastically as they moved from the testis to the caput epididymidis. Thereafter, only little and insignificant changes were observed. Testicular sperm was composed more of the fastest anodically-migrating isoenzyme (LDH1) while with sperm maturation, the least or slowest migrating isoenzymes (LDH4 and 5) became progressively more dominant. This loss in LDH content in sperm and the shifts in the LDH isoenzyme patterns indicate that the development of sperm during maturation is dependent on a delicate balance between lactate and pyruvate, such that the cathodic isoenzymes involved in the anaerobic energy-supplying metabolic processes are sufficiently available for sperm activity and survival.