The heterogeneity of the protamines from human spermatozoa.

Nuclear basic protein from ejaculated human spermatozoa were labelled with iodo[14C1]acetic acid and fractionated by ion-exchange chromatography into several pools (named A-K). Gel electrophoresis indicated that the minor protamine components, were present in pool D and that, of the major protamine components, component 1 (pools E, F, G, H) was well separated from the unresolved mixture of component 2 and component 3 (pools I, J, K). Pools G and J were free of other contaminants. Pools D, G, and J produced different radioactive peptides on digestion with trypsin and with thermolysin, and also had quite distinct amino acid compositions. This suggests that the heterogeneity of human protamines is caused by differences in amino acid sequence. Major component 1 also seems to be heterogenous, since it was found in two distinct peaks (pools E and G), but post-translational modification as a cause of the two types of component 1 has not been ruled out. Although all the human protamine components are similar to other mammalian protamines in containing half-cysteine and tyrosine, they also have unique common features such as high histidine and high glutamic acid contents.