Molecules of histones H1 isolated from the calf thymus, carp testicles and spermatozoa as well as trypsin-stable fragments of these proteins have been studied from the standpoint of their structure and interaction using methods of differential spectrophotometry, gel filtration and turbidimetry. The globular structure of histone H1 of the calf thymus is formed with an increase in the ionic strength of the medium and it is eluted as dimer with gel chromatography. With a considerable local increase of ionic strength (by addition of NaCl crystals) molecules of histones H1 form high-molecular aggregates from all the studied tissues. This aggregation is a result of interaction of globular trypsin-stable sites. Molecules of histone H1 from carp testicles and spermatozoa as well as their trypsin-stable fragments revealed no differences in the ability to form dimers and aggregates.
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