The characterization and molecular structure of hepatoproliferin: a liver regeneration factor from rat hepatocytes.

Hepatoproliferin (HPF) was purified from regenerating rat livers as an oligomeric entity (big-HPF) from which the monomeric form (small-HPF) could be obtained using disaggregating conditions. By using a solid-phase ion-exchange method, small-HPF was forced to dissociate into two charged ionic species, namely norepinephrine (NE) and a sulfonated disaccharide with a molecular structure consisting of D-glucuronic acid bound to glucosamine 2,6-disulfate by a beta-glycosidic linkage having a beta, 1 --> 4 configuration. Monomeric HPF stemmed from the formation of three electrostatic bonds between the protonated amine groups of three norepinephrines, of which two bind to the deprotonated sulfonic groups of glucosamine 2,6-disulfate and one to the deprotonated carboxylic group of glucuronic acid, to constitute a tightly associated complex with a molecular mass of 1046 Da.

Oligomeric hepatoproliferin disaggregates into an active monomer that was purified and forcefully dissociated into two different ionic species.

Hepatoproliferin (HPF), a liver regeneration factor, was isolated initially as an aggregated molecule (big-HPF) and was purified into two homogeneous, bioactive species of 14 kDa and 18.5 kDa. These two big-HPFs were disaggregated to completion into two monomeric forms (small-HPFs) when incubated for 10 days in 0.

The prevalence and purification of hepatoproliferin: a liver regeneration factor from rat hepatocytes.

Hepatoproliferin (HPF), a liver regeneration factor that was able to augment the growth of hepatocytes in the presence of EGF, was produced by young rat livers and hepatectomized adult livers (70%), but not by adult intact livers. Therefore only growing and regenerating livers produce HPF. This growth factor was purified into two homogeneous bioactive species having different single SDS-PAGE bands at 18.