The Applications of Genetic Modification.
Since ancient times, man has been using living organisms for industrial purposes, for example, to make yoghurt and cheese from milk you need bacteria (containing chymosin for cheese). Bread and beer are made from cereals using yeast.
Transgenic animals capable of producing useful recombinant proteins are the latest of biotechnological developments.
"A Transgenic animal has had a gene (or genes) either removed or added to its genome" .
(Dr Ed Wraith, 11/2002).
Introduced genes, called transgenes, come form a species different from the host organism. By carrying this extra piece of DNA, an animal can synthesise proteins normally produced by other species. This has been possible in bacteria and organisms such as yeast for several decades.
All proteins are synthesised form only 20 different amino acids. The composition of a specific protein is determined by the way different amino acids are linked together in a chain. This sequence is in turn determined by the genes, which provide the template that dictates that every molecule of an individual protein is identical.
This means you could produce theoretically limitless amounts of specific proteins. This means that the gene sequences isolated from any organism could be introduced into bacteria, which are capable of producing large amounts of protein.
In this way, proteins that are rare could be produced for industrial applications (e.g. enzymes in washing powders) or medical treatments (e.g. drugs to dissolve blood clots). New proteins could also be designed, or natural proteins modified, to produce tailor-made proteins for specific uses. However it is extremely difficult to manipulate due to the complex nature of proteins themselves and how cells make them.
The 20 natural occurring amino acids could be in theory be ordered in any sequence to give an infinite number of potential proteins. The correct amino acid sequence is crucial for the protein to adopt the right 3-D Shape and fulfil its function.
