By October 1945, DDT was available for public sale in the United States, used both as an agricultural pesticide and as a household insecticide.  Although its use was promoted by government and the agricultural industry, US scientists such as FDA pharmacologist Herbert O. Calvery expressed concern over possible hazards associated with DDT as early as 1944.    As its production and use increased, public response was mixed. At the same time that DDT was hailed as part of the "world of tomorrow," concerns were expressed about its potential to kill harmless and beneficial insects (particularly pollinators ), birds, fish, and eventually humans. The issue of toxicity was complicated, partly because DDT's effects varied from species to species, and partly because consecutive exposures could accumulate, causing damage comparable to large doses. A number of states attempted to regulate DDT.   In the 1950s the federal government began tightening regulations governing its use.  These events received little attention. Women like Dorothy Colson and Mamie Ella Plyler of Claxton, Georgia gathered evidence about DDT's effects and wrote to the Georgia Department of Public Health, the National Health Council in New York City, and other organizations. 
The relative binding affinities of testosterone (T), 19-nortestosterone (N) and their 5 alpha-reduced derivatives: 5 alpha-dihydrotestosterone (DHT) and 5 alpha-dihydro-19-nortestosterone (DHN) to the androgen receptor of the rat seminal vesicle was studied using competition experiments. In cell-free extracts incubated at +10 degrees C for 18 h the relative binding affinities of these steroids (DHT greater than T = DHN = N) proved to be specific for the androgen receptor, in the sense that only prostatic extracts gave a similar result while three other androgen binding proteins (human sex steroid binding globulin, rat epididymal androgen binding protein and an antibody raised against T) exhibited quite different binding specificities. In minced seminal vesicles incubated at 37 degrees C for 1 h the binding affinities showed marked differences (DHT greater than N greater than T greater than or equal to DHN) and similar patterns were observed with both the cytoplasmic and the nu clear receptors. Our findings suggest that (I) the simultaneous presence of a 4-ene double bond and 19-methyl group in T does not favor the tight binding of T to the androgen receptor; therefore, either saturation of this double bond or elimination of the 19-methyl group leads to increased binding and (II) while 5 alpha-reduction of T increases the affinity of this steroid to the receptor, that of N does not influence or rather tends to decrease the binding affinity. The opposite changes observed in the binding affinities of T and N after their 5 alpha-reduction may account for the lower androgenicity of N. On the other hand, the relative myotropic activity in vivo of these steroids is apparently determined by the ratio of their affinities (N/T approximately 3 at 37 degrees C) to the androgen receptor.