OwensResearch paperPhenylketonuria: PKUPhenylketonuria also known as PKU once had irrevocable and detrimental damage to the people it effected. Babies that were born with the genetic disorder were certain to suffer from severe mental retardation and behavioral disorders because no one knew what was causing the symptoms. Until 1934 when a biochemist and doctor named A. Folling from Norway discovered the disease through urine testing.(Mange,4) He identified that it was a hereditary disease which causes the affected person’s body to not be able to handle a substance called phenylalanine (phe), an essential amino acid found in protein. After Folling’s discovery of the disease, in 1947 George Jervis, an American scientist finally presented that the exact cause was an enzyme found in the liver called Phenylalnine hydroxylase (PAH). PAH is responsible for converting excess phenylalanine into tyrosine and other useful amino acids. Tyrosine is an essential amino acid that makes proteins, hormones and neurotransmitters that control brain functions. The discovery of the mutant PAH enzyme made it possible to start searching for a treatment. It was reasoned that by removing foods which contained phe from the affected person’s diet and giving them vitamin supplements would stop the toxic effect of excess phe and its derivatives in the body. Doctors quickly saw profound effects in the diet therapy and now patients, when treated soon after birth can develop normally by sticking to a medical diet.(Mange, 346)PKU is a autosomal recessive inherited condition with phenotypic characteristics that prevent affected individuals from normally metabolizing phenylalanine (phe). Untreated, this hereditary biochemical disorder prevents normal brain development and usually results in severe mental retardation. Other phenotypic symptoms are skin rash, seizures, excessive restlessness, irritable behavior and sometimes a musty or mousy b...
