The isolation and partial characterization of diphosphoglycerate mutase from human erythrocytes

Kappel, William K.; Hass, Louis F.

doi:10.1021/bi00647a008

Cited by 49 publications

(10 citation statements)

References 33 publications

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“…One of these enzymes is the 2,3-bisphosphoglycerate synthasephosphatase or 2,3-bisphosphoglycerate mutase (EC 5.4.2.4), which is a homodimer of a subunit that possesses great homology with PGM subunits (Sasaki et al, 1975;Kappel and Hass, 1976;Sasaki et al, 1976;Narita et al, 1979). The other two enzyme proteins are heterodimers resulting from the combination of a BPGM subunit with a PGM subunit either type M or type B Pons et al, 1985a).…”

Section: Discussionmentioning

confidence: 99%

Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activity and isoenzymes in lung, colon and liver carcinomas

Durany

Joseph²,

Campo³

et al. 1997

Br J Cancer

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SummaryWe have compared the levels of phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activities and the distribution of their isoenzymes in normal colon, liver and lung tissues, and in colon, liver and lung adenocarcinoma, lung squamous cell carcinoma and lung carcinoid. All tumours presented higher phosphoglycerate mutase and enolase activities and lower 2,3-bisphosphoglycerate phosphatase activity than the normal tissues. No changes were observed in the phosphoglycerate mutase isoenzyme patterns analysed by cellulose acetate electrophoresis. All specimens contained mainly type BB isoenzyme, traces of type MB isoenzyme and no type MM isoenzyme. However, the tumours had decreased levels of 2,3-bisphosphoglycerate mutase and 2,3-bisphosphoglycerate mutase-phosphoglycerate mutase hybrid enzyme. Determined by agarose gel electrophoresis, aa-enolase was the isoenzyme predominant in normal lung, colon and liver tissue, although ay-and yy-enolase were also present in all tissues. In colon, liver and non-endocrine lung tumours, the proportions of ay-and yy-enolase decreased. In contrast, in carcinoid tumours of the lung, the proportions of these isoenzymes increased.Keywords: 2,3-bisphosphoglycerate mutase; 2,3-bisphosphoglycerate phosphatase; enolase; phosphoglycerate mutase; isoenzyme; lung, colon and liver adenocarcinoma; lung squamous cell carcinoma; lung carcinoid Phosphoglycerate mutase (D-phosphoglycerate 2,3-phosphomutase, EC 5.4.2.1, PGM) and enolase (2-phospho-D-glycerate hydrolyase, EC 4.2.1.11) are glycolytic enzymes that catalyse consecutive reversible reactions connecting the two ATP-generating reactions in the glycolytic pathway. PGM catalyses the conversion of 3-phosphoglycerate, product of the first ATP-generating reaction, into 2-phosphoglycerate in the presence of the cofactor 2,3-bisphosphoglycerate. Enolase catalyses the conversion of 2-phosphoglycerate into phosphoenolpyruvate, substrate of the second ATP-generating reaction. In addition to the main mutase activity, PGM possesses collateral 2,3-bisphosphoglycerate synthase or 2,3-bisphosphoglycerate mutase activity (BPGM: 1,3-bisphosphoglycerate + 3-phosphoglycerate -> 3-phosphoglycerate + 2,3-bisphosphoglycerate) and 2,3-bisphosphoglycerate phosphatase activity (BPGP: 2,3-bisphosphoglycerate --3-phosphoglycerate + Pi), which is stimulated by 2-phosphoglycolate (for reviews, see Fothergill-Gilmore and Watson, 1989;Wold, 1971).In mammalian tissues, there are three isoenzymes of PGM, which result from the homodimeric and the heterodimeric combinations of two different subunits coded by separate genes and designated M (muscle) and B (brain). In early fetal life, type BB-PGM is the only form present. During myogenesis, the isoenzyme phenotype undergoes transition, type BB-PGM being replaced by the MM-form, through the MB isoenzyme. In skeletal muscle, there is an almost complete transition from the BB-to the MM-PGM, but in heart muscle complete transition does not occur (Omenn and Cheung, Omenn and Hermodson, 1975;Adamson, 1...

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Section: Discussionmentioning

confidence: 99%

Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activity and isoenzymes in lung, colon and liver carcinomas

Durany

Joseph²,

Campo³

et al. 1997

Br J Cancer

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“…(7,8). The trifunctional enzyme has been obtained in a purified form by the use of chromatographic techniques (9,10). This enzyme presents a single electrophoretic band (6) and represents one of the three molecular forms of erythrocyte MPGM (8).…”

Section: Introductionmentioning

confidence: 99%

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

Rosa¹,

Prehu²,

Beuzard³

et al. 1978

J. Clin. Invest.

116

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“…The ratio between the activities of 2,3-P,glycerate phosphatase and 2,3-P,glycerate mutase were the same in both fractions. These data are interpreted as demonstrating that the 2,3-P2-glycerate phosphatase-mutase of the day-old chick erythrocyte possesses inherent 3-Pglycerate mutase activity as has been shown both for the enzyme from human erythrocytes purified to homogeneity [4,5] and that from equine erythrocytes [6].…”

Section: 3-p2glycerate Phosphatase Activity and 23-p2glycerate Conmentioning

confidence: 76%

“…The precipitate formed at 80% saturation had a ratio of 3-Pglycerate mutase : 2,3-P2glycerate mutase activities of 1.3, suggesting a small contamination with one of the other isozymes of 3-Pglycerate mutase in this precipitate. Kappel and Hass [5] reported that 3-Pglycerate mutase of human erythrocytes precipitates at a higher ammonium sulfate concentration than does 2,3-P,-glycerate mutase. Sasaki et al [4] found that their most highly purified 2,3-P2glycerate phosphatase-mutase preparation contained equal amounts of 2,3-P2glycer-ate mutase and 3-P glycerate mutase activities although Kappel and Hass [5] and Rose and Whalen [2] reported considerably lower 3-f glycerate mutase activity in their most highly purified preparations.…”

Section: Discussionmentioning

confidence: 98%

Purification and Properties of 2,3-Bisphosphoglycerate Phosphatase-Mutase from Erythrocytes of Day-Old Chicks

1977

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1. Large quantities of 2,3-bisphosphoglycerate accumulate in the red blood cells of the chick embryo during the week prior to hatching; the 2,3-bisphosphoglycerate then abruptly decreases to very small amounts within a few days after hatching.2. The enzyme 2,3-bisphosphoglycerate phosphatase was purified from the red blood cells of the day old chick. The elution profiles for bisphosphoglycerate phosphatase and 2,3-bisphosphoglycerate mutase were identical upon gradient elution from columns of hydroxylapatite and diethylaminoethylcellulose and by gel filtration on Sephadex G-100. At each stage of purification the ratio of phosphatase to mutase activity was the same. It was concluded that, just as in the human erythrocyte, both bisphosphoglycerate phosphatase and 2,3-bisphosphoglycerate mutase activities in chick erythrocytes reside on one protein.3. Bisphosphoglycerate phosphatase has a pH of optimal activity of 7.0. Its activity is stimulated by 2-phosphoglycolate, phosphoenolpyruvate, bisulfite and dithionite and is inhibited by 2-phosphoglycerate, 3-phosphoglycerate, inorganic pyrophosphate and phytic acid. These properties are very similar to those described for bisphosphoglycerate phosphatase purified from human erythrocytes.4. The purified bisphosphoglycerate phosphatase-mutase contained 3-phosphoglycerate mutase activity. Although the 2,3-bisphosphoglycerate mutase and 3-phosphoglycerate mutase activities were nearly equal in the purified enzyme, this protein accounts for a maximum of only 6% of the 3-phosphoglycerate mutase activity in these cells.

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The isolation and partial characterization of diphosphoglycerate mutase from human erythrocytes

Cited by 49 publications

References 33 publications

Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activity and isoenzymes in lung, colon and liver carcinomas

Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activity and isoenzymes in lung, colon and liver carcinomas

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

Purification and Properties of 2,3-Bisphosphoglycerate Phosphatase-Mutase from Erythrocytes of Day-Old Chicks

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