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"zinc phosphate cement"¿¡ ´ëÇÑ °Ë»ö °á°úÀÔ´Ï´Ù. °Ë»ö °á°ú º¸´Â µµÁß¿¡ Tab ۸¦ ´©¸£½Ã¸é °Ë»ö âÀÌ ¼±Åõ˴ϴÙ.
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ZPP zinc protoporphyrin
ZTT zinc turbidity test
ADP Adenosine Di-Phosphate
AMP Adenosine Mono-Phosphate
ATP   1) Adenosine Tri-Phosphate
  2) Autoimmune Thrombocytopenic Purpura
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PAP 3'(2')-phosphoadenosine 5'-phosphate
PAPS 3'-phosphate 5'-phosphosulfate
PAPS 3'-phosphate 5'-phosphosulphate
InsP 3)H]inositol phosphate
[(3)H]InsP 3)H]inositol phosphate
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 8
glucose-1-phosphate adenylyltransferase <enzyme> Shrunken-2 (sh2) protein is a subunit of this enzyme
Registry number: EC 2.7.7.27
Synonym: adpg synthetase, adpglucose pyrophosphorylase, ADP-glucose synthetase, shrunken-2 protein, shrunken gene product, ADP-glucose pyrophosphorylase, glgc gene product, bt2 gene product, brittle-2 gene product
(26 Jun 1999)
glucose-1-phosphate kinase <enzyme> An enzyme that, in the presence of ATP, catalyses the phosphorylation of d-glucose 1-phosphate to form d-glucose 1,6-bisphosphate and ADP; found in yeast and muscle; d-glucose 1,6-bisphosphate is a required cofactor of one of the enzymes in glycogenolysis.
Synonym: glucose-1-phosphate kinase.
(05 Mar 2000)
glucose-1-phosphate phosphodismutase A phosphotransferase catalyzing the reversible transfer of a phosphate residue from one d-glucose 1-phosphate to another, yielding d-glucose 1,6-bisphosphate and d-glucose. This enzyme provides a crucial intermediate needed for glucose-phosphate isomerase.
(05 Mar 2000)
glucose-1-phosphate uridylyltransferase <enzyme> An enzyme that activates d-glucose by reacting d-glucose 1-phosphate with UTP, producing pyrophosphate and UDP glucose; a crucial step in glycogen biosynthesis.
(05 Mar 2000)
glucose-6-phosphate <biochemistry> Glucose 6-phosphate is a phosphomonoester of glucose that is formed by transfer of phosphate from ATP, catalysed by the enzyme hexokinase.
It is an intermediate both of the glycolytic pathway (next converted to fructose 6 phosphate) and of the NADPH generating pentose phosphate pathway, formed from glucose via hexokinase. However it is not strictly a glycolytic intermediate and it is readily converted to glycogen or oxidized to NADPH.
(10 Oct 1997)
glucose-6-phosphate dehydrogenase <enzyme> An NADP+ enzyme that catalyses the dehydrogenation (oxidation) of d-glucose-6-phosphate to 6-phospho-d-glucono-d-lactone, this reaction initiating the Dickens shunt.
Deficiency of this enzyme is the commonest disease-causing enzyme defect in humans affecting an estimated 400 million people.
The gene for this enzyme is on the X chromosome. Males with the enzyme deficiency develop haemolytic anaemia when red blood cells are exposed to oxidant drugs such as the antimalarial primaquine, the sulfonamide antibiotics or sulfones, naphthalene moth balls, or fava beans.
Synonym: Robison ester dehydrogenase, Zwischenferment.
Acronym: G6PD
(12 Sep 2002)
glucose-6-phosphate dehydrogenase deficiency A deficiency of glucose-6-phosphate dehydrogenase, an enzyme important for maintaining cellular concentrations of reduced nucleotides.
Deficiency of this enzyme is the commonest disease-causing enzyme defect in humans affecting an estimated 400 million people.
The gene for this enzyme is on the X chromosome and there are various polymorphic forms.
Males with the enzyme deficiency develop haemolytic anaemia when red blood cells are exposed to oxidant drugs such as the antimalarial primaquine, the sulfonamide antibiotics or sulfones, naphthalene moth balls, or fava beans. It can also cause anaemia of the newborn, and chronic nonspherocytic haemolytic anaemia.
Inheritance: X-linked.
(12 Sep 2002)
glucose-6-phosphate isomerase <enzyme> An enzyme that catalyses the reversible interconversion of glucose-6-phosphate and fructose-6-phosphate, and is a part of the glycolytic and gluconeogenic pathways. Deficiency of the enzyme, an autosomal recessive trait, results in liver glycogenesis and haemolytic anaemia.
Chemical name: D-Glucose-6-phosphate ketol-isomerase
Registry number: EC 5.3.1.9
(12 Dec 1998)
glucose-6-phosphate translocase <enzyme> A component of EC 3.1.3.9 which transports glucose phosphate into endoplasmic reticulum
Registry number: EC 2.7.-
Synonym: t1 transport protein
(26 Jun 1999)
glucose-phosphate isomerase <enzyme> An enzyme that catalyses the reversible interconversion of d-fructose 6-phosphate and d-glucose-6-phosphate; a part of glycolysis and gluconeogenesis; glucosephosphate isomerase deficiency is an inherited disorder resulting in liver glycogenesis and haemolytic anaemia.
Synonym: hexosephosphate isomerase, phosphohexomutase, phosphohexose isomerase.
(05 Mar 2000)
glucosylglycerol-phosphate phosphatase <enzyme> Isolated from synechocystis; do not confuse with stpa protein from e. Coli
Registry number: EC 3.1.3.-
Synonym: stpa gene product, synechocystis
(26 Jun 1999)
glutamine-fructose-6-phosphate transaminase (isomerizing) <enzyme> An enzyme that catalyses the synthesis of fructose-6-phosphate plus glutamine from glutamate plus glucosamine-6-phosphate.
Chemical name: L-Glutamine:D-fructose-6-phosphate aminotransferase (hexose-isomerizing)
Registry number: EC 2.6.1.16
(12 Dec 1998)
glyceraldehdye 3 phosphate <biochemistry> Three carbon intermediate of the glycolytic pathway formed by the cleavage of fructose 1,6 bisphosphate, catalysed by the enzyme aldolase.
Also involved in reversible interchange between glycolysis and the pentose phosphate pathway.
(18 Nov 1997)
glyceraldehyde 3-phosphate <biochemistry> In glycolysis, glyceraldehyde 3-phosphate is created from dihydroxyacetone phosphate with the aid of triose-phosphate isomerase. In turn, it an dorganic phosphate and NAD+ are converted into 1,3-bisphosphoglycerate, NADH and free hydrogen with the aid of glyceraldehyde 3-phosphate dehydrogenase.
(09 Oct 1997)
glyceraldehyde 3-phosphate dehydrogenase <biochemistry> In glycolysis, this enzyme catalyses the conversion of glyceraldehyde 3-phosphate and organic phosphate and NAD+ into 1,3-bisphosphoglycerate and NADH and free hydrogens (and viceversa) by transferring hydrogens and electrons between the molecules.
(09 Oct 1997)
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