Proteolysis

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    Aneurysm Essay

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    Introduction Despite considerable advances in surgical treatment, the ruptured human abdominal aortic aneurysm (AAA) is still associated with a mortality rate of 65–85% [1, 2] . A diameter is currently the only reliable determinant of the imminent rupture of an AAA and patients exceeding 5.5 cm generally undergo surgical or endovascular intervention [2, 3] . However, the outcome of rupture is poor with less than half of the patients being delivered to the hospital alive [1, 4] . It is well known

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    Proteolysis in Cheese Ripening: Proteolysis is one of the most complex biochemical events in cheese ripening that contributes to the typical taste, texture, and aroma of every cheese variety. This fundamental process in cheese ripening is caused by agents from several sources such as indigenous milk enzymes, lasting coagulant, and enzymes from secondary flora. As a result of its importance, proteolysis has been a key subject of active analysis in the past decade as new evaluation techniques are

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    Conventional surfactant: Traditionally various chemical process are carried out to synthesis most of the commercial surfactant. Petrochemicals are being used as raw materials for production of surfactant, due to their huge availability, cost, and performance. For example some petrochemical are as follows paraffin, benzene, olefin fatty alcohol, fatty acid, and ethanol-amine, ethylene oxide, propyl-oxide etc. Limitation of Conventional surfactant: 1. Toxic by-product formation: a very complex reaction

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    substances as: proteoses, peptones, polypeptides, and amino acids. These are all simple proteins or base amino acids that are easily decomposed . Later in the decay of the body, structures like reticulin, muscle protein, and collagen start to experience proteolysis too. These proteins take longer to decompose because of their complexity. The continuing breakdown of proteins can lead to the production of the gases carbon dioxide, hydrogen sulphide (which is toxic), ammonia, and methane. When the amino acids

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    Millions of Americans undergo elective surgery. For many years overnight fasting, up to 12 hrs had been the recommended routine before elective surgery. This practice was instituted to reduce gastric acidity and to reduce the gastric volume for the risk of aspiration of stomach contents and during anesthesia. Patients who had stayed NPO for twelve hours have an increase in anxiety, thirst and fatigue. The combination of anxiety, thirst and fatigue led to poor patient satisfaction and resulted in

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    proteins (Davis et.al., 1998) that form the catalytic core in the protease γ-secretase (Francis et.al., 2002), which is responsible for the proteolysis of APP (Navivaeva & Turner, 2013). When there is a mutation at the loci for PSEN1 and PSEN2, located on chromosome 14 and 1 respectively, the activity of γ-secretase is altered resulting in changes in the proteolysis of APP and increased formation of Aβ (Qain et.al., 1998). Due to the increase of Aβ, amyloid plaques aggregate quickly causing early-onset

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    Enzyme Protease. A disease is the destruction in the function of a human which leads to specific symptoms which in turn affects specific sites and are not results of physical injury. Protease cleaves longer proteins into shorter core proteins via proteolysis this is the process whereby hydrolysis of the peptide bonds occur that links subsequent amino acids to a polypeptide chain (Kohei Oda 2012). It is therefore crucial for the effectiveness of an infectious virus. Protease Inhibitors bind to the active

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    Researches about Huntington’s disease (HD) revealed that it is caused by an expanded CAG trinucleotide repeat in HTT, the gene responsible for expressing the protein huntingtin. It was also revealed that the reduced expression of this protein leads to the neurodegenerative effects of the disease. However, the pathophysiology of the disease is still unknown. This paper investigated the pathophysiology of Huntington’s disease. This paper is based upon the toxic peptide theory of the disease pathogenesis

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    the mid-1980’s by Aaron Ciechhanover, Avram Hershko, and Irwin Rose, which helped them win the Nobel Prize for Chemistry in 2004 (Nobel Prize website). Initially, the process was looked at as proteolytic system utilizing ATP. Many ATP-dependent proteolysis factor 1 (APF-1) molecules linked with a substrates that were later found to be deteriorated with free APF-1 in the cellular extract (Ciechhanover, 2012). APF-1 was called ubiquitin and it uses its C-terminal glycine to conjugate to the substrate’s

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    where it is activated into trypsin by proteolytic cleavage and forms chains of trypsin. Trypsin’s function is to separate the peptide chains at the carboxyl side, of lysine and arginine. This process is referred to as trypsinisation or trypsin proteolysis. This process allows the absorbing of proteins in food because peptides are too large to be absorbed by the final section of the small intestine, ileum. Trypsin works at the carboxyl side of the amino acid because if there’s any acidic silt left

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