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Ascaris Lumbricoides4
''Ascaris'' is a nematode genus of parasitic worms known as the "small intestinal roundworms". One species, ''Ascaris lumbricoides'', affects humans and causes the disease ascariasis. Another species, ''Ascaris suum'', typically infects pigs. Other ascarid genera infect other animals, such as ''Parascaris equorum'', the equine roundworm, and ''Toxocara'' and ''Toxascaris'', which infect dogs and cats. Their eggs are deposited in feces and soil. Plants with the eggs on them infect any organism that consumes them. ''A. lumbricoides'' is the largest intestinal roundworm and is the most common helminth infection of humans worldwide. Infestation can cause morbidity by compromising nutritional status, affecting cognitive processes, inducing tissue reactions such as granuloma to larval stages, and by causing intestinal obstruction, which can be fatal. Morphology and Anatomy * Adult: cylindrical shape, creamy white or pinkish in color * Male: average ; more slender than the female * ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Carl Linnaeus
Carl Linnaeus (23 May 1707 – 10 January 1778), also known after ennoblement in 1761 as Carl von Linné,#Blunt, Blunt (2004), p. 171. was a Swedish biologist and physician who formalised binomial nomenclature, the modern system of naming organisms. He is known as the "father of modern Taxonomy (biology), taxonomy". Many of his writings were in Latin; his name is rendered in Latin as and, after his 1761 ennoblement, as . Linnaeus was the son of a curate and was born in Råshult, in the countryside of Småland, southern Sweden. He received most of his higher education at Uppsala University and began giving lectures in botany there in 1730. He lived abroad between 1735 and 1738, where he studied and also published the first edition of his ' in the Netherlands. He then returned to Sweden where he became professor of medicine and botany at Uppsala. In the 1740s, he was sent on several journeys through Sweden to find and classify plants and animals. In the 1750s and 1760s, he co ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Pseudocoelom
A body cavity is any space or compartment, or potential space, in an animal body. Cavities accommodate organs and other structures; cavities as potential spaces contain fluid. The two largest human body cavities are the ventral body cavity, and the dorsal body cavity. In the dorsal body cavity the brain and spinal cord are located. The membranes that surround the central nervous system organs (the brain and the spinal cord, in the cranial and spinal cavities) are the three meninges. The differently lined spaces contain different types of fluid. In the meninges for example the fluid is cerebrospinal fluid; in the abdominal cavity the fluid contained in the peritoneum is a serous fluid. In amniotes and some invertebrates the peritoneum lines their largest body cavity called the coelom. Mammals Mammalian embryos develop two body cavities: the intraembryonic coelom and the extraembryonic coelom (or chorionic cavity). The intraembryonic coelom is lined by somatic and splanchnic ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Carboxypeptidase Inhibitor
A carboxypeptidase ( EC number 3.4.16 - 3.4.18) is a protease enzyme that hydrolyzes (cleaves) a peptide bond at the carboxy-terminal (C-terminal) end of a protein or peptide. This is in contrast to an aminopeptidases, which cleave peptide bonds at the N-terminus of proteins. Humans, animals, bacteria and plants contain several types of carboxypeptidases that have diverse functions ranging from catabolism to protein maturation. At least two mechanisms have been discussed. Functions Initial studies on carboxypeptidases focused on pancreatic carboxypeptidases A1, A2, and B in the digestion of food. Most carboxypeptidases are not, however, involved in catabolism. Instead they help to mature proteins, for example post-translational modification. They also regulate biological processes, such as the biosynthesis of neuroendocrine peptides such as insulin requires a carboxypeptidase. Carboxypeptidases also function in blood clotting, growth factor production, wound healing, reproduction ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Metallocarboxypeptidase
A metalloexopeptidase is a type of enzyme that acts as a metalloproteinase exopeptidase. These enzymes have a catalytic mechanism involving a metal, often zinc. They function in molecular biology as agents that cut the terminal (or penultimate) peptide bonds ending peptide chains. Analogous to slicing the end off a loaf of bread, the process releases a single amino acid (or dipeptide) for use. Metallocarboxypeptidase The terms "metallo carboxypeptidase", "metallo-carboxypeptidase" and "metallocarboxypeptidase" are used to describe a metalloexopeptidase carboxypeptidase. These peptidases specifically target the C-terminus, the unbound carboxyl group (-COOH) at one distinct end of the amino acid chain (cutting one side from a loaf of bread rather than the end). Enzyme Commission number Using the Enzyme Commission number (EC number) system, metallocarboxypeptidases fall under EC 3.4.17. Examples of these compounds in the human genome include AGBL1 and AGBL2, known also as AT ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cathepsin
Cathepsins (Ancient Greek ''kata-'' "down" and ''hepsein'' "boil"; abbreviated CTS) are proteases (enzymes that degrade proteins) found in all animals as well as other organisms. There are approximately a dozen members of this family, which are distinguished by their structure, catalytic mechanism, and which proteins they cleave. Most of the members become activated at the low pH found in lysosomes. Thus, the activity of this family lies almost entirely within those organelles. There are, however, exceptions such as cathepsin K, which works extracellularly after secretion by osteoclasts in bone resorption. Cathepsins have a vital role in mammalian cellular turnover. Classification * Cathepsin A (serine protease) * Cathepsin B (cysteine protease) * Cathepsin C (cysteine protease) * Cathepsin D ( aspartyl protease) * Cathepsin E (aspartyl protease) * Cathepsin F (cysteine proteinase) * Cathepsin G (serine protease) * Cathepsin H (cysteine protease) * Cathepsin K (cyste ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Elastase
In molecular biology, elastase is an enzyme from the class of proteases (peptidases) that break down proteins, specifically one that can break down elastin. In other words, the name only refers to the substrate specificity (i.e. what proteins it can digest), not to any kind of evolutionary grouping. Forms and classification Eight human genes exist for elastase: The four "pancreatic elastases", chymotrypsin, and neutrophil elastase are serine proteases. The "macrophage elastase" is a matrix metallopeptidase. Chymotrypsin is weaker at digesting elastin than the architypical pancreatic elastase. Some bacteria (including ''Pseudomonas aeruginosa'') also produce elastase; bacterial elestases work in many ways and include serine proteases, aspartic proteases, thiol proteases, and metalloenzymes. Function The fact that elastase can break down elastin in test tubes (while other proteases cannot) does not imply that there is a unifying function for all elastases in the living ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Chymotrypsin
Chymotrypsin (, chymotrypsins A and B, alpha-chymar ophth, avazyme, chymar, chymotest, enzeon, quimar, quimotrase, alpha-chymar, alpha-chymotrypsin A, alpha-chymotrypsin) is a digestive enzyme component of pancreatic juice acting in the duodenum, where it performs proteolysis, the breakdown of proteins and polypeptides. Chymotrypsin preferentially cleaves peptide amide bonds where the side chain of the amino acid N-terminal to the scissile amide bond (the P1 position) is a large hydrophobic amino acid ( tyrosine, tryptophan, and phenylalanine). These amino acids contain an aromatic ring in their side chain that fits into a hydrophobic pocket (the S1 position) of the enzyme. It is activated in the presence of trypsin. The hydrophobic and shape complementarity between the peptide substrate P1 side chain and the enzyme S1 binding cavity accounts for the substrate specificity of this enzyme. Chymotrypsin also hydrolyzes other amide bonds in peptides at slower rates, particularly th ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Trypsin
Trypsin is an enzyme in the first section of the small intestine that starts the digestion of protein molecules by cutting long chains of amino acids into smaller pieces. It is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyzes proteins. Trypsin is formed in the small intestine when its proenzyme form, the trypsinogen produced by the pancreas, is activated. Trypsin cuts peptide chains mainly at the carboxyl side of the amino acids lysine or arginine. It is used for numerous biotechnological processes. The process is commonly referred to as trypsinogen proteolysis or trypsinization, and proteins that have been digested/treated with trypsin are said to have been trypsinized. Trypsin was discovered in 1876 by Wilhelm Kühne. Although many sources say that Kühne named trypsin from the Ancient Greek word for rubbing, 'tripsis', because the enzyme was first isolated by rubbing the pancreas with glass powd ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Pepsin
Pepsin is an endopeptidase that breaks down proteins into smaller peptides and amino acids. It is one of the main digestive enzymes in the digestive systems of humans and many other animals, where it helps digest the proteins in food. Pepsin is an aspartic protease, using a catalytic aspartate in its active site. It is one of three principal endopeptidases (enzymes cutting proteins in the middle) in the human digestive system, the other two being chymotrypsin and trypsin. There are also exopeptidases which remove individual amino acids at both ends of proteins (carboxypeptidases produced by the pancreas and aminopeptidases secreted by the small intestine). During the process of digestion, these enzymes, each of which is specialized in severing links between particular types of amino acids, collaborate to break down dietary proteins into their components, i.e., peptides and amino acids, which can be readily absorbed by the small intestine. The cleavage specificity o ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Proteases
A protease (also called a peptidase, proteinase, or proteolytic enzyme) is an enzyme that catalyzes proteolysis, breaking down proteins into smaller polypeptides or single amino acids, and spurring the formation of new protein products. They do this by cleaving the peptide bonds within proteins by hydrolysis, a reaction where water breaks bonds. Proteases are involved in numerous biological pathways, including digestion of ingested proteins, protein catabolism (breakdown of old proteins), and cell signaling. In the absence of functional accelerants, proteolysis would be very slow, taking hundreds of years. Proteases can be found in all forms of life and viruses. They have independently evolved multiple times, and different classes of protease can perform the same reaction by completely different catalytic mechanisms. Classification Based on catalytic residue Proteases can be classified into seven broad groups: * Serine proteases - using a serine alcohol * Cysteine prot ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Sexual Dimorphism
Sexual dimorphism is the condition where sexes of the same species exhibit different Morphology (biology), morphological characteristics, including characteristics not directly involved in reproduction. The condition occurs in most dioecy, dioecious species, which consist of most animals and some plants. Differences may include secondary sex characteristics, size, weight, color, markings, or behavioral or cognitive traits. Male-male reproductive competition has evolved a diverse array of sexually dimorphic traits. Aggressive utility traits such as "battle" teeth and blunt heads reinforced as battering rams are used as weapons in aggressive interactions between rivals. Passive displays such as ornamental feathering or song-calling have also evolved mainly through sexual selection. These differences may be subtle or exaggerated and may be subjected to sexual selection and natural selection. The opposite of dimorphism is ''monomorphism'', when both biological sexes are phenotype, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Embryo
An embryo ( ) is the initial stage of development for a multicellular organism. In organisms that reproduce sexually, embryonic development is the part of the life cycle that begins just after fertilization of the female egg cell by the male sperm cell. The resulting fusion of these two cells produces a single-celled zygote that undergoes many cell divisions that produce cells known as blastomeres. The blastomeres (4-cell stage) are arranged as a solid ball that when reaching a certain size, called a morula, (16-cell stage) takes in fluid to create a cavity called a blastocoel. The structure is then termed a blastula, or a blastocyst in mammals. The mammalian blastocyst hatches before implantating into the endometrial lining of the womb. Once implanted the embryo will continue its development through the next stages of gastrulation, neurulation, and organogenesis. Gastrulation is the formation of the three germ layers that will form all of the different parts of t ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
