insulin: Isolation and Structure
Frederick G. Banting , Charles H. Best , and J. J. R. Macleod were the first to obtain, from extracts of pancreas (1921–22), a preparation of insulin that could serve to replace a deficiency of the hormone in the human body. The complete amino acid sequence of the insulin molecule was described in the early 1950s; insulin was the first protein to be sequenced entirely. This pioneering work was confirmed from 1963 to 1966, when several groups reported laboratory synthesis of biologically active insulin. The three-dimensional structure of the crystalline hormone was published in 1969.
Insulin has been shown to be a protein consisting of two polypeptide chains (see peptide ), one of 21 amino acid residues and the other of 30, joined by two disulfide bridges (see cysteine ). The two chains are synthesized in the β cells as part of one continuous polypeptide chain called proinsulin; a 32-amino acid sequence (the connecting peptide) is subsequently split out of the proinsulin molecule by an enzyme resembling trypsin to yield active insulin.
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