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Immunocyanin
Hemocyanins (also spelled haemocyanins and abbreviated Hc) are proteins that transport oxygen throughout the bodies of some invertebrate animals. These metalloproteins contain two copper atoms that reversibly bind a single oxygen molecule (O2). They are second only to hemoglobin in frequency of use as an oxygen transport molecule. Unlike the hemoglobin in red blood cells found in vertebrates, hemocyanins are not confined in blood cells but are instead suspended directly in the hemolymph. Oxygenation causes a color change between the colorless Cu(I) deoxygenated form and the blue Cu(II) oxygenated form. Species distribution Hemocyanin was first discovered in '' Octopus vulgaris'' by Leon Fredericq in 1878. The presence of copper in molluscs was detected even earlier by Bartolomeo Bizio in 1833. Hemocyanins are found in the Mollusca and Arthropoda including cephalopods and crustaceans and utilized by some land arthropods such as the tarantula ''Eurypelma californic ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Octopus
An octopus ( : octopuses or octopodes, see below for variants) is a soft-bodied, eight- limbed mollusc of the order Octopoda (, ). The order consists of some 300 species and is grouped within the class Cephalopoda with squids, cuttlefish, and nautiloids. Like other cephalopods, an octopus is bilaterally symmetric with two eyes and a beaked mouth at the center point of the eight limbs. The soft body can radically alter its shape, enabling octopuses to squeeze through small gaps. They trail their eight appendages behind them as they swim. The siphon is used both for respiration and for locomotion, by expelling a jet of water. Octopuses have a complex nervous system and excellent sight, and are among the most intelligent and behaviourally diverse of all invertebrates. Octopuses inhabit various regions of the ocean, including coral reefs, pelagic waters, and the seabed; some live in the intertidal zone and others at abyssal depths. Most species grow quickly, mature ea ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cephalopod
A cephalopod is any member of the molluscan class Cephalopoda (Greek plural , ; "head-feet") such as a squid, octopus, cuttlefish, or nautilus. These exclusively marine animals are characterized by bilateral body symmetry, a prominent head, and a set of arms or tentacles (muscular hydrostats) modified from the primitive molluscan foot. Fishers sometimes call cephalopods "inkfish", referring to their common ability to squirt ink. The study of cephalopods is a branch of malacology known as teuthology. Cephalopods became dominant during the Ordovician period, represented by primitive nautiloids. The class now contains two, only distantly related, extant subclasses: Coleoidea, which includes octopuses, squid, and cuttlefish; and Nautiloidea, represented by ''Nautilus'' and ''Allonautilus''. In the Coleoidea, the molluscan shell has been internalized or is absent, whereas in the Nautiloidea, the external shell remains. About 800 living species of cephalopods have been ident ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Peptide
Peptides (, ) are short chains of amino acids linked by peptide bonds. Long chains of amino acids are called proteins. Chains of fewer than twenty amino acids are called oligopeptides, and include dipeptides, tripeptides, and tetrapeptides. A polypeptide is a longer, continuous, unbranched peptide chain. Hence, peptides fall under the broad chemical classes of biological polymers and oligomers, alongside nucleic acids, oligosaccharides, polysaccharides, and others. A polypeptide that contains more than approximately 50 amino acids is known as a protein. Proteins consist of one or more polypeptides arranged in a biologically functional way, often bound to ligands such as coenzymes and cofactors, or to another protein or other macromolecule such as DNA or RNA, or to complex macromolecular assemblies. Amino acids that have been incorporated into peptides are termed residues. A water molecule is released during formation of each amide bond.. All peptides except cyclic pep ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
N-terminus
The N-terminus (also known as the amino-terminus, NH2-terminus, N-terminal end or amine-terminus) is the start of a protein or polypeptide, referring to the free amine group (-NH2) located at the end of a polypeptide. Within a peptide, the amine group is bonded to the carboxylic group of another amino acid, making it a chain. That leaves a free carboxylic group at one end of the peptide, called the C-terminus, and a free amine group on the other end called the N-terminus. By convention, peptide sequences are written N-terminus to C-terminus, left to right (in LTR writing systems). This correlates the translation direction to the text direction, because when a protein is translated from messenger RNA, it is created from the N-terminus to the C-terminus, as amino acids are added to the carboxyl end of the protein. Chemistry Each amino acid has an amine group and a carboxylic group. Amino acids link to one another by peptide bonds which form through a dehydration reaction that ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Zymogen
In biochemistry, a zymogen (), also called a proenzyme (), is an inactive precursor of an enzyme. A zymogen requires a biochemical change (such as a hydrolysis reaction revealing the active site, or changing the configuration to reveal the active site) for it to become an active enzyme. The biochemical change usually occurs in Golgi bodies, where a specific part of the precursor enzyme is cleaved in order to activate it. The inactivating piece which is cleaved off can be a peptide unit, or can be independently-folding domains comprising more than 100 residues. Although they limit the enzyme's ability, these N-terminal extensions of the enzyme or a “prosegment” often aid in the stabilization and folding of the enzyme they inhibit. The pancreas secretes zymogens partly to prevent the enzymes from digesting proteins in the cells in which they are synthesised. Enzymes like pepsin are created in the form of pepsinogen, an inactive zymogen. Pepsinogen is activated when chief ce ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Diptera
Flies are insects of the order Diptera, the name being derived from the Greek δι- ''di-'' "two", and πτερόν ''pteron'' "wing". Insects of this order use only a single pair of wings to fly, the hindwings having evolved into advanced mechanosensory organs known as halteres, which act as high-speed sensors of rotational movement and allow dipterans to perform advanced aerobatics. Diptera is a large order containing an estimated 1,000,000 species including horse-flies, crane flies, hoverflies and others, although only about 125,000 species have been described. Flies have a mobile head, with a pair of large compound eyes, and mouthparts designed for piercing and sucking (mosquitoes, black flies and robber flies), or for lapping and sucking in the other groups. Their wing arrangement gives them great maneuverability in flight, and claws and pads on their feet enable them to cling to smooth surfaces. Flies undergo complete metamorphosis; the eggs are often laid on the l ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Phenoloxidase
Polyphenol oxidase (PPO; also polyphenol oxidase i, chloroplastic), an enzyme involved in fruit browning, is a tetramer that contains four atoms of copper per molecule. PPO may accept monophenols and/or ''o''-diphenols as substrates. The enzyme works by catalyzing the ''o''-hydroxylation of monophenol molecules in which the benzene ring contains a single hydroxyl substituent to ''o''-diphenols (phenol molecules containing two hydroxyl substituents at the 1, 2 positions, with no carbon between). It can also further catalyse the oxidation of ''o''-diphenols to produce ''o''-quinones. PPO catalyses the rapid polymerization of ''o''-quinones to produce black, brown or red pigments (polyphenols) that cause fruit browning. The amino acid tyrosine contains a single phenolic ring that may be oxidised by the action of PPOs to form ''o''-quinone. Hence, PPOs may also be referred to as tyrosinases. Common foods producing the enzyme include mushrooms (''Agaricus bisporus''), appl ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Superfamily (proteins)
SUPERFAMILY is a database and search platform of structural and functional annotation for all proteins and genomes. It classifies amino acid sequences into known structural domains, especially into SCOP superfamilies. Domains are functional, structural, and evolutionary units that form proteins. Domains of common Ancestry are grouped into superfamilies. The domains and domain superfamilies are defined and described in SCOP. Superfamilies are groups of proteins which have structural evidence to support a common evolutionary ancestor but may not have detectable sequence homology. Annotations The SUPERFAMILY annotation is based on a collection of hidden Markov models (HMM), which represent structural protein domains at the SCOP superfamily level. A superfamily groups together domains which have an evolutionary relationship. The annotation is produced by scanning protein sequences from completely sequenced genomes against the hidden Markov models. For each protein you can: * S ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Scutigera Coleoptrata
''Scutigera coleoptrata'', also known as the house centipede, is a species of centipede that is typically yellowish-grey and has up to 15 pairs of long legs. Originating in the Mediterranean region, it has spread to other parts of the world, where it can live in human homes. It is an insectivore; it kills and eats other arthropods, such as insects and arachnids. Etymology In 1758, Carl Linnaeus described the species in the tenth edition of his Systema Naturae, giving the name ''Scolopendra coleoptrata'', writing that it has a "coleopterated thorax" (similar to a coleopter). In 1801, Jean-Baptiste Lamarck separated ''scutigera'' from ''scolopendra'', calling this species ''Scutigera coleoptrata.'' The word ''scutigera'' comes from "to bear" (''gerere)'' and "shield" (''scutum),'' because of the shape of the plates in the back of the chilopod. Morphology The body of an adult ''Scutigera coleoptrata'' is typically in length, although larger specimens are sometimes encountered. ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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