Intensive insulin therapy and microvascular disease) is central to the development of complications of diabetes mellitus. This evidence convinced most physicians who specialize in diabetes care that an important goal of treatment is to make the biochemical profile of the diabetic patient (blood lipids, HbA1c, etc.) as close to the values of non-diabetic people as possible. This is especially true for young patients with many decades of life ahead. A working pancreas continually secretes small amounts of insulin into the blood to maintain normal glucose levels, which would otherwise rise from glucose release by the liver, especially during the early morning dawn phenomenon.
Insulin suggests that it has been conserved across much of animal evolutionary history. The C-peptide of proinsulin (discussed later), however, differs much more among species; it is also a hormone, but a secondary one. The primary structure of bovine insulin was first determined by Frederick Sanger in 1951. After that, this polypeptide was synthesized independently by several groups. The 3-dimensional structure of insulin was determined by X-ray crystallography in Dorothy Hodgkin's laboratory in 1969 (PDB file 1ins). Insulin is produced and stored in the body as a hexamer (a unit of six insulin molecules), while the active form is the monomer.