2,3-Diphosphoglycerate Phosphatase from Human Erythrocytes

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The purification and properties of diphosphoglycerate mutase from human erythrocytes.

where PGA is phosphoglyceric acid. The kinetic studies with the human enzyme indicate K, values of 0.53 FM for 1,3-diphosphoglycerate and 1 to 1.5 PM for 3-phosphoglycerate. 2,3-Diphosphoglycerate is a competitive inhibitor of 1,3-diphosphoglycerate with a Ki of 0.85 FM; it is noncompetitive with 3-phosphoglycerate. Inorganic phosphate inhibits competitively with 3-phosphoglycerate with a Ki of...

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The Purification and Properties of Diphosphoglycerate Mutase from Human Erythrocytes*

where PGA is phosphoglyceric acid. The kinetic studies with the human enzyme indicate K, values of 0.53 FM for 1,3-diphosphoglycerate and 1 to 1.5 PM for 3-phosphoglycerate. 2,3-Diphosphoglycerate is a competitive inhibitor of 1,3-diphosphoglycerate with a Ki of 0.85 FM; it is noncompetitive with 3-phosphoglycerate. Inorganic phosphate inhibits competitively with 3-phosphoglycerate with a Ki of...

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In vivo aging of transfused erythrocytes and 2,3-diphosphoglycerate levels.

Levels of 2,3-diphosphoglycerate (2,3-DPG) of the hematocrit decreased. On five and oxygen affinity were measured in a separate occasions, the 2,3-DPG concentrapatient with refractory congenital hypotion was elevated (average 25.5 , moles/g plastic anemia in order to determine the of hemoglobin) and the P50 level increased response of aging transfused erythrocytes (average 33.2 mm of mercury) 2...

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The first case of a complete deficiency of diphosphoglycerate mutase in human erythrocytes.

An inherited and complete deficiency of diphosphoglycerate mutase was discovered in the erythrocytes of a 42-yr-old man of French origin whose blood hemoglobin concentration was 19.0 g/dl. Upon physical examination he was normal with the exception of a ruddy cyanosis. The morphology of his erythrocytes was also normal and there was no evidence of hemolysis. The erythrocyte 2,3-diphosphoglycerat...

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Myosin from human erythrocytes.

We have purified myosin from human erythrocytes using methods similar to that for other cytoplasmic myosins with a yield of about 500 micrograms/100 ml of packed cells. It consists of a 200-kDa heavy chain and light chains of 26- and 19.5 kDa and therefore differs from the isozyme in platelets which has light chains of 20- and 15 kDa. At low ionic strength, the myosin forms short bipolar filame...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1970

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)63045-5