i would think they could due to the fact that more than one codon can code for an amino acid
The immune system can distinguish animal insulin from human insulin due to differences in their amino acid sequences. While insulin from different species is quite similar, even small variations can be recognized by the immune system's antibodies and T-cells, which are trained to identify foreign proteins. This recognition can lead to an immune response, making animal insulin less effective or potentially triggering allergic reactions in humans.
The amino acid sequences of hemoglobin in humans and frogs are different due to evolutionary divergence. While both hemoglobins are composed of similar building blocks (amino acids), the specific sequence of amino acids varies between species. This divergence in sequence reflects the adaptation of these proteins to meet the specific oxygen-carrying needs of each species.
The human gene that codes for insulin is inserted into bacteria to produce insulin. The gene is typically inserted into a plasmid vector, which allows the bacteria to express the human insulin gene and produce insulin. This technique is used in biotechnology to create recombinant bacteria that can produce insulin for medical use.
Yes, human insulin can be produced through genetically engineered organisms, such as transgenic bacteria or yeast. These organisms are modified to express the human insulin gene, allowing them to produce insulin that is identical to the insulin produced by humans.
Insulin is a protein secreted in pancreas.
They changed the amino acid sequence of the proteins.
yes. amino acids can be coded for by more that one codon. https://www.msu.edu/course/lbs/145/smith/s04/graphics/campbell_17.4.gif
The gene of insulin has a different sequence of molecular bases than the gene of testosterone.
The immune system can distinguish animal insulin from human insulin due to differences in their amino acid sequences. While insulin from different species is quite similar, even small variations can be recognized by the immune system's antibodies and T-cells, which are trained to identify foreign proteins. This recognition can lead to an immune response, making animal insulin less effective or potentially triggering allergic reactions in humans.
they worked backwards from mRNA to DNA Ap#x
the subunits that proteins are made from are called amino acids , there are about 20 common amino acids that are used in the synthesis of proteins in humans , and proteins differ in the number , types , and sequence of amino acids .
gm insulin is specific to humans unlike animal insulin which is specific to that animal
The amino acid sequences of hemoglobin in humans and frogs are different due to evolutionary divergence. While both hemoglobins are composed of similar building blocks (amino acids), the specific sequence of amino acids varies between species. This divergence in sequence reflects the adaptation of these proteins to meet the specific oxygen-carrying needs of each species.
Almost every essential function in humans is carried out by proteins; all humans need proteins.
The human gene that codes for insulin is inserted into bacteria to produce insulin. The gene is typically inserted into a plasmid vector, which allows the bacteria to express the human insulin gene and produce insulin. This technique is used in biotechnology to create recombinant bacteria that can produce insulin for medical use.
Humans, who are not diabetic, make the insulin they need within their own bodies.
Genetic mutations over time likely caused changes in the amino acid sequence from gorillas to humans. These mutations could have arisen from environmental factors, natural selection, or genetic drift. As a result, differences in amino acids between gorillas and humans have accumulated over millions of years of evolution.