Question

how DNA recombinant technology is important to produce human growth hormone with figure, explanation, and advantages

Answer 1

Recombinant DNA is a form of DNA constructed in the laboratory. It is generated by transferring selected pieces of DNA from one organism to another.

Genetic engineering is used for many different purposes in research, medicine, agriculture and industry. The technology is important because it enables the creation of multiple copies of genes and the insertion of foreign genes into other organisms to give them new traits, such as antibiotic resistance or a new colour. One of the first ways in which the technology was deployed was to re-engineer microbial cells to produce foreign proteins. This facilitated the manufacture of human proteins on an unprecedented scale at minimum cost, thereby opening the way to study the function of proteins in greater detail and to their therapeutic use. By 2001 over 80 recombinant DNA based products had been approved for treating disease and for vaccination and a further 350 recombinant DNA-based drugs were being tested for safety and efficacy. The technology is also an important tool in agriculture, being used to improve plants' resistance to pests and increase crop yields.

While the structure of DNA was first determined in 1953, it was to take another two decades before scientists had the means to generate recombinant DNA. This was aided by firstly the realisation in the 1950s that plasmids, small mobile pieces of DNA, could replicate in huge quantities independently of chromosomal bacteria DNA and that they could transfer genetic information. It was this process that gave host bacteria the capacity to inherit new genes and therefore new functions such as resistance to antibiotics. Another important tool for creating recombinant DNA was the discovery in the 1960s by the Swiss microbiologist Werner Arber and American biochemist Stuart Linn that bacteria could protect themselves from attack by viruses the production of endonucleases, known as restriction enzymes, which could seek out a single DNA sequence in a virus and cut it precisely in one place. This process prevented the replication of viruses and hence the death of virally infected bacteria. The first restriction enzyme, Escscherichia coli K, was isolated and purified in 1968 by Matthew Meselson and Robert Yuan at Harvard University. Two years later Hamilton O Smith, Thomas Kelly and Kent Welcox at Johns Hopkins University isolated and characterised the first site-specific restriction enzyme, later named HindII. This was demonstrated by Daniel Nathans to be a useful tool for cutting and pasting specific DNA segments. The first protocol for creating recombinant DNA was put forward in the early 1970s by Peter Lobban and Armin Dale Kaiser at Stanford University Medical School. In 1971 Paul Berg, attached to Stanford University, demonstrated the feasibility of splicing and recombining genes for the first time. Two years later, Stanley Cohen and Herbert Boyer, based respectively at Stanford University and University of California at San Francisco, successfully inserted recombinant DNA into bacteria for replication.

Gene cloning has a diverse range of applications. Where it has proven particularly useful has been in mapping out the human genome, the creation of transgenic animals, and the development of insect-resistant crops. It is also pivotal to genetic tests carried out in forensic science and archaeology as well as in tests for determining hereditary disease and paternity. The technology also forms the backbone of hepatitis and human immunodeficiency virus (HIV) diagnostic tests. Recombinant DNA technology has also proven important to the production of vaccines and protein therapies such as human insulin, interferon and human growth hormone. It is also used to produce clotting factors for treating haemophilia and in the development of gene therapy.

A variety of diseases are treated using rDNA proteins derived from humans or other animals. Insulin, for example, is used to treat diabetes. Before the development of rDNA technology, these proteins had to be produced by isolating them from human or animal tissue, an expensive and difficult process. Today, however, these substances can be produced in bacteria by using rDNA technology, which makes them more affordable and easily available. Human growth hormone and insulin are two of many proteins produced in this way.

efore rDNA technology, hepatitis B vaccines used weakened or killed hepatitis viruses to stimulate a response from the human immune system. Newer vaccines use hepatitis B proteins produced with rDNA technology. As a result, vaccines now contain only a small amount of protein from the virus rather than a virus itself. The protein is completely noninfectious and unlike the virus poses no risk of causing an infection. Today, some scientists work with similar rDNA techniques to develop vaccines for other diseases such as influenza. Flu vaccines have traditionally been manufactured in chicken eggs, so people with egg allergies can't take them. Vaccines produced with rDNA methods don't have these limitations.

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