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Giant Intestinal Roundworm
''Ascaris'' is a genus of parasitic nematode worms known as the "small intestinal roundworms", which is a type of parasitic worm. One species, ''Ascaris lumbricoides'', affects humans and causes the disease ascariasis. Another species, ''Ascaris suum'', typically infects pigs. ''Parascaris equorum'', the equine roundworm, is also commonly called an "ascarid". 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 * Adult: cylindrical shape, creamy white or pinkish in color * Male: average 15–30 cm (6–12 inches); more slender than the female * Female: average 20–35&n ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Carl Linnaeus
Carl Linnaeus (; 23 May 1707 – 10 January 1778), also known after his ennoblement in 1761 as Carl von Linné Blunt (2004), p. 171. (), was a Swedish botanist, zoologist, taxonomist, and physician who formalised binomial nomenclature, the modern system of naming organisms. He is known as the "father of modern taxonomy". Many of his writings were in Latin; his name is rendered in Latin as and, after his 1761 ennoblement, as . Linnaeus was born in Råshult, the countryside of Småland, in 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 continued to collect an ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Proteases
A protease (also called a peptidase, proteinase, or proteolytic enzyme) is an enzyme that catalyzes (increases reaction rate or "speeds up") 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 many biological functions, 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. Hierarchy of proteases Based on catalytic residue Proteases can be classified into seven broad groups: * Serine proteases - ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ascaridida
The order Ascaridida includes several families of parasitic roundworms with three "lips" on the anterior end. They were formerly placed in the subclass Rhabditia by some, but morphological and DNA sequence data rather unequivocally assign them to the Spiruria. The Oxyurida and Rhigonematida are occasionally placed in the Ascaridida as superfamily Oxyuroidea, but while they seem indeed to be Spiruria, they are not as close to ''Ascaris'' as such a treatment would place them.Tree of Life Web Project (ToL) (2002)Nematoda Version of 2002-JAN-01. Retrieved 2008-NOV-02. These "worms" contain a number of important parasites of humans and domestic animals. Important families include: * The Anisakidae are also called the "marine mammal ascarids". The larvae of these worms cause anisakiasis when ingested by humans in raw or insufficiently cooked fish, but do not reproduce in humans. * The Ascarididae include the giant intestinal roundworms (''Ascaris'' spp.). * The Cosmocercidae include ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
List Of Parasites (human)
Endoparasites Protozoan organisms Helminths (worms) Helminth organisms (also called helminths or intestinal worms) include: Tapeworms Flukes Roundworms Other organisms Ectoparasites References {{Portal bar, Biology, Medicine * Parasites Parasitism is a Symbiosis, close relationship between species, where one organism, the parasite, lives on or inside another organism, the Host (biology), host, causing it some harm, and is Adaptation, adapted structurally to this way of lif ... * ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Edward Tyson
Edward Tyson (20 January 1651 – 1 August 1708) was an English scientist and physician. He is commonly regarded as the founder of modern comparative anatomy, which compares the anatomy between species. Biography Tyson was born the son of Edward Tyson at Clevedon, in Somerset. He became a BA from Oxford on 8 February 1670, an MA from Oxford on 4 November 1673, and an MD from Cambridge in 1678. He was admitted to the College of Physicians on 30 September 1680 and as a Fellow in April 1683. In 1684 he was appointed physician and governor to the Bethlem Hospital in London (the first mental hospital in Britain and the second in Europe). He is credited with changing the hospital from a zoo of sorts to a place intended to assist its inmates. He was elected a Fellow of the Royal Society in November 1679. He is buried at St Dionis Backchurch. Anatomical research In 1680, Tyson studied a porpoise and established that it is a mammal. He noted that the convoluted structures of the brains ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Mummy
A mummy is a dead human or an animal whose soft tissues and organs have been preserved by either intentional or accidental exposure to chemicals, extreme cold, very low humidity, or lack of air, so that the recovered body does not decay further if kept in cool and dry conditions. Some authorities restrict the use of the term to bodies deliberately embalmed with chemicals, but the use of the word to cover accidentally desiccated bodies goes back to at least 1615 AD (see the section Etymology and meaning). Mummies of humans and animals have been found on every continent, both as a result of natural preservation through unusual conditions, and as cultural artifacts. Over one million animal mummies have been found in Egypt, many of which are cats. Many of the Egyptian animal mummies are sacred ibis, and radiocarbon dating suggests the Egyptian Ibis mummies that have been analyzed were from time frame that falls between approximately 450 and 250 BC. In addition to the mummies ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Paleofeces
Paleofeces (or palaeofaeces in British English) are ancient human feces, often found as part of archaeological excavations or surveys. The term coprolite is often used interchangeably, although coprolite can also refer to fossilized animal feces. Intact feces of ancient people may be found in caves in arid climates and in other locations with suitable preservation conditions. They are studied to determine the diet and health of the people who produced them through the analysis of seeds, small bones, and parasite eggs found inside. The feces can contain information about the person excreting the material as well as information about the material itself. They can also be chemically analyzed for more in-depth information on the individual who excreted them, using lipid analysis and ancient DNA analysis. The success rate of usable DNA extraction is relatively high in paleofeces, making it more reliable than skeletal DNA retrieval. The reason this analysis is possible at all i ... [...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, reproduct ... [...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 ATP/G ... [...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 (cysteine protea ... [...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. In particular, it is a serine protease. Forms and classification Eight human genes exist for elastase: Some bacteria (including ''Pseudomonas aeruginosa'') also produce elastase. In bacteria, elastase is considered a virulence factor. Function Elastase breaks down elastin, an elastic fibre that, together with collagen, determines the mechanical properties of connective tissue. The neutrophil form breaks down the ''Outer membrane protein A'' (OmpA) of '' E. coli'' and other Gram-negative bacteria. Elastase also has the important immunological role of breaking down Shigella virulence factors. This is accomplished through the cleavage of peptide bonds in the target proteins. The specific peptide bonds cleaved are those on the carboxyl side of small, hydrophobic amino acids such as glycine, alanine, and valine. For more on how this is accomplished, see serine p ... [...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 tho ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
