Human Serum Albumin

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HUMAN SERUM ALBUMIN (1E78) The Structure and Significance of Human Serum Albumin in Blood

May 11, 2013
Human Serum Albumin (H.S. Albumin) is the most common transporting protein found in blood plasma. Its Y-shaped molecule is mostly build of α-helix configurations that are perfect sites for carrying hydrophobic organic compounds. The human organism highly depends on the proper functioning of H. S. Albumin, thus its function and nature have been extensively studied. This article briefly describes H. S. Albumin structural features and how they influence albumin’s transposing mechanism.

Introduction Proteins are large polypeptide molecules consisting of chains of amino acids. The order of amino acids in each protein is determined by the codon of the nucleotide acid sequence that is encoded within the organism’s genetic material. The combination of amino acid sequence influences how the protein will fold into its specific, three-dimensional structure. In turn, the protein’s three-dimensional structure will highly influence the physical and chemical activity of that protein. Proteins perform all major functions within living organisms. One of these functions is transportation of molecules from one location to another. Human serum albumin is a common protein in human blood responsible for transporting metabolite products, lipids and drugs. Human serum albumin makes total of 62% of all proteins in blood plasma[i], and belongs to serum albumin family produced by human liver. Because of its abundance in blood plasma, human serum albumin was first protein that had been discovered and intensively studied. According to Academic Press, serum albumin was first precipitated from urine in the1500s by Paracelsus, and was later crystallized by A. Gürber in 1894 (Peters…...

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