No other isomer or isotope of gold has three decay paths. Synthesis
The possible production of gold from a more common element, such as lead, has long been a subject of human inquiry, and the ancient and medieval discipline of alchemy often focused on it; however, the transmutation of the chemical elements did not become possible until the understanding of nuclear physics in the 20th century. The first synthesis of gold was conducted by Japanese physicist Hantaro Nagaoka, who synthesized gold from mercury in 1924 by neutron bombardment. An American team, working without knowledge of Nagaokas prior study, conducted the same experiment in 1941, achieving the same result and showing that the isotopes of gold produced by it were all radioactive. In 1980, Glenn Seaborg transmuted several thousand atoms of bismuth into gold at the Lawrence Berkeley Laboratory. Gold can be manufactured in a nuclear reactor, but doing so is highly impractical and would cost far more than the value of the gold that is produced. Chemistry
Although gold is the most noble of the noble metals, it still forms many diverse compounds. The oxidation state of gold in its compounds ranges from −1 to +5, but Au(I) and Au(III) dominate its chemistry. Au(I), referred to as the aurous ion, is the most common oxidation state with soft ligands such as thioethers, thiolates, and organophosphines. Au(I) compounds are typically linear. A good example is Au(CN)−2, which is the soluble form of gold encountered in mining.
Hemoglobinemia (or haemoglobinaemia) is a medical condition in which there is an excess of hemoglobin in the blood plasma. This is an effect of intravascular hemolysis, in which hemoglobin separates from red blood cells, a form of anemia. Hemoglobinemia can be caused by intrinsic or extrinsic factors. When hemoglobinemia is internally caused, it is a result of recessive genetic defects that cause the red blood cells to lyse, letting the hemoglobin spill out of the cell into the blood plasma. In intravascular hemolysis, hemoglobin is released and binds with haptoglobin. This causes haptoglobin levels to decrease. Once haptoglobin is saturated, free hemoglobin readily distributes to tissues where it might be exposed to oxidative conditions. In such conditions, heme can be released from ferric hemoglobin. The free heme can then accelerate tissue damage by promoting peroxidative reactions and activation of inflammatory cascades. Hemopexin (Hx) is another plasma glycoprotein able to bind heme with high affinity. Hx sequesters heme in an inert, non-toxic form and transports it to the liver for catabolism and excretion. As long as both haptoglobin and hemopexin are saturated, the remaining free hemoglobins are filtered in the kidney and some of them will be reabsorbed by way of proximal tubules. In externally caused hemoglobinemia, an outside attacker acts as an antibody against the red blood cells. This can cause the cells to be destroyed and their hemoglobin released.