The surname Cox is of English or Welsh origin, and may have originated independently in several places in Great Britain, with the variations arriving at a standard spelling only later. There are also two native Irish surnames which were anglicised into Cox.
An early record of the surname dates from 1556 with the marriage of Alicea Cox at St. Martin in the Fields, Westminster, London. Cox is the 69th-most common surname in the United Kingdom.
One possibility of the origin is that it is a version of the Old English cocc which means "the little", and was sometimes put after the name of a leader or chieftain as a term of endearment. Surnames such as Wilcox, Willcocks and Willcox are examples of this practice: all are composed of the name William and the archaic word cocc, coming together to mean "little William". The suggestion is that only the element -cox may have endured as a surname for some families.
Another opinion is that the name is derived from the Old English cock, which means a "heap" or "mound", and was a topographic name for a man living near any heap, hill or other bundle. Names like Haycock or Haycox come from such practice, meaning from "the hay mounds" or "the hay fields". Again, the element -cox may have only been carried on in some families.
Cytochrome c oxidase subunit 2, also known as cytochrome c oxidase polypeptide II, is a protein that in humans is encoded by the MT-CO2 gene.
Cytochrome c oxidase subunit II, abbreviated COXII, COX2, COII, or MT-CO2, is the second subunit of cytochrome c oxidase.
Cytochrome c oxidase (EC 1.9.3.1) is an oligomeric enzymatic complex which is a component of the respiratory chain and is involved in the transfer of electrons from cytochrome c to oxygen. In eukaryotes this enzyme complex is located in the mitochondrial inner membrane; in aerobic prokaryotes it is found in the plasma membrane. The enzyme complex consists of 3-4 subunits (prokaryotes) to up to 13 polypeptides (mammals). In Leigh's disease, there may be an abnormality or deficiency of cytochrome oxidase.
Subunit 2 (COII) transfers the electrons from cytochrome c to the catalytic subunit 1. It contains two adjacent transmembrane regions in its N-terminus and the major part of the protein is exposed to the periplasmic or to the mitochondrial intermembrane space, respectively. COII provides the substrate-binding site and contains a copper centre called Cu(A) (see IPR001505), probably the primary acceptor in cytochrome c oxidase. An exception is the corresponding subunit of the cbb3-type oxidase which lacks the copper A redox-centre. Several bacterial COII have a C-terminal extension that contains a covalently bound haem c.
Prostaglandin-endoperoxide synthase 2 (prostaglandin G/H synthase and cyclooxygenase) (The HUGO official symbol is PTGS2; HGNC ID, HGNC:9605), also known as cyclooxygenase-2 or COX-2, is an enzyme that in humans is encoded by the PTGS2 gene. Because the "COX" term is used for the stem symbol for "cytochrome c oxidase" family of genes and gene products including proteins, the "PTGS" symbol is used for the prostaglandin-endoperoxide synthase (cyclooxygenase) family of genes and proteins. It is involved in the conversion of arachidonic acid to prostaglandin H2, an important precursor of prostacyclin and thromboxane A2, among others.
PTGS2 (COX-2) was discovered in 1991 by the Daniel Simmons laboratory at Brigham Young University.
PTGS2 (COX-2), converts arachidonic acid (AA) to prostaglandin endoperoxide H2. PGHSs are targets for NSAIDs and PTGS2 (COX-2) specific inhibitors called coxibs. PGHS-2 is a sequence homodimer. Each monomer of the enzyme has a peroxidase and a PTGS (COX) active site. The PTGS (COX) enzymes catalyze the conversion of arachidonic acid to prostaglandins in a two steps. First, hydrogen is abstracted from carbon 13 of arachidonic acid, and then two molecules of oxygen are added by the PTGS2 (COX-2), giving PGG2. Second, PGG2 is reduced to PGH2 in the peroxidase active site. The synthesized PGH2 is converted to prostaglandins (PGD2, PGE2, PGF2α), prostacyclin (PGI2), or thromboxane A2 by tissue-specific isomerases.(Figure 2)
Robert Chase, M.D. is a fictional character on the Fox medical drama House. He is portrayed by Jesse Spencer. His character was a part of the team of diagnosticians who worked under Gregory House until the end of the third season when House fires him. However, he resumed work at the hospital as a surgeon, and was re-hired by House in season 6. Robert Chase is the longest-serving member of House's staff. Chase has been attracted to Allison Cameron since the beginning of the show and embarks on a romantic relationship with her in "Human Error." In "Post Mortem," he left the Diagnostic Team after realizing he was in the same position as he was 10 years earlier, unlike all of the other former members of the team. However, in the series finale, he rejoins the hospital as the new Head of Diagnostic Medicine, replacing House, who is thought to have died.
An Australian, Chase is portrayed as an eager fellow of House during the first 3 seasons, often supporting his opinions and carrying out his orders without question. He was raised Catholic, and in the Season 1 episode "Damned If You Do," it was revealed that he attended seminary before becoming a doctor. He seems to trust House the most and sometimes takes part in House's morally questionable plans when the other members of the team have refused, showing a situational application of ethics and a flexible stance on morality. This leads to tension between Chase and Foreman, who is quick to disagree with House and prove him wrong.
Chase is a given name and surname in the English language, especially in the United States. The given name is a transferred use of the surname.
In the United Kingdom a chase is a type of common land used for hunting to which there are no specifically designated officers and laws but instead reserved hunting rights for one or more persons. Similarly, a Royal Chase is a type of Crown Estate by the same description, but where certain rights are reserved for a member of the British Royal Family.
Examples of chases in England include the Wyre Forest that straddles the border of Worcestershire and Shropshire, Malvern Chase in Worcestershire, and Pensnett Chase near Dudley.
Cannock Chase in Staffordshire has reverted to a chase (which like most chases has been partly reduced in size by settlements). It was in the Middle Ages a Royal Forest, although it merged with a chase around Beaudesert originally belonging (in most of the Middle Ages) to the Bishop of Lichfield.
The Victoria County History describes a chase as:
Chases, often with more clearings than forests for hunting purposes, or due to their soil type, such as more heath, faced mass inclosure by Private (specifically local) Acts of Parliament primarily throughout the heyday of that type of privatisation 1600-1850. Inclosure converted from to some extent public to private land many chases. The private land after this has in many areas been converted, in part to residential, commercial, industrial or transport infrastructure use, however the chases listed here (see examples) remain largely undiminished by staying a common or by a gift to a public body whether to avoid inheritance tax or motivated by philanthropy.