[Analytical ion-exchange and gel chromatography of radioisotope-labeled protein (polypeptide) hormones]

On the example of prolactin-I125 the author presents his experience in the use of gel filtration and ion-exchange chromatography for complete characterization of homogeneity and immunological properties of labeled hormones preparations. These methods can be used in studying various aspects of protein and polypeptide hormones metabolism, including various stages of their action mechanism, and also to characterize the hormones manufactured. It was shown that the formation of prolactin complex with gamma-globulins was accompanied by additional polarization of the hormone molecules, this leading to an increased energy of interaction with the ion exchange surface. The effect of polarization of the hormone molecules on the biological properties of the hormones themselves, their complexes with serum proteins and membrane receptors is discussed.