The scope of this review is restricted to the chemistry of the nonsteroid hormones, inasmuch as the chemistry of the steroid hormones is presented elsewhere in this volume. Moreover, the rather comprehensive review of hormone chemistry by Wettstein & Benz (1) in the previous volume of the Annual Review of Biochemistry has made it possible to limit this chapter al most entirely to publications which have appeared within the last 18 months. References to earlier work will be made only for the sake of continuity of the presentation.
INSULINInterest in the chemistry of insulin has continued particularly in the ap plication of the newer techniques of protein analysis in order to obtain more information regarding the structure of this protein hormone. The papers reviewed here have been selected from those which have appeared since the review by Wettstein & Benz (1), which devoted a good deal of attention to the more recent work on the chemistry of insulin.The behavior of insulin in the ultracentrifuge has been studied in two laboratories. Gutfreund (2) confirmed his previous observations (3), based on osmotic pressure measurements, that insulin in solutions of pH 7.0 to 7.5 and a concentration of 0.4 to 0.9 per cent was homogeneous from the point of view of particle size, and had a maximum molecular weight of 47,000 to 48,000. However, at pH above 7.5 or below 4.0, or in more dilute solutions, evidence was obtained for reversible dissociation of the protein hormone. The optimum pH for dissociation was between 2 and 3. Under the influence of the combined effect of pH, dilution and temperature, the minimum molec ular weight from osmotic pressure determinations was 12,000 ±500. Similar data (12,000 ±530) with respect to minimum � olecular weight were obtained by calculations based on amino acid analysis. It was concluded that insulin consists of subunits with a molecular weight of 12,000 and that the forces holding these subunits together involve the ionizing groups of the protein.Observations of this dissociation phenomenon by osmotic pressure and ultra centrifugal methods are in good agreement. Oncley & Ellenbogen (4), using the ultracentrifuge, studied the molecular state of insulin as a function of the insulin concentration, the pH, and the ionic strength of the solution in order to examine the forces involved in the polymerization of the insulin subunit of molecular weight 12,000. The data showed that the sedimentation con stant was a function of the net charge of the insulin and the ionic strength of the solution. The monomer of molecular weight 12,000 had a maximum net 1 Miss Annette Terzian gave invaluable assistance in the assembling of the litera ture upon which this review is based.
261Annu. Rev. Biochem. 1950.19:261-276. Downloaded from www.annualreviews.org Access provided by University of California -San Francisco UCSF on 02/07/15. For personal use only.Quick links to online content Further ANNUAL REVIEWS