Effects of salts and pH on the rate of erythrocyte diphosphoglycerate mutase

Rose, Zelda B.

doi:10.1016/0003-9861(73)90585-7

Cited by 44 publications

(25 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The bisphosphoglyceromutase activity was inhibited by 2,3-bisphosphoglycerate, potassium phosphate, bisulfite or 2-phosphoglycolate. These effects are in agreement with the results reported previously [6,7,9,22], although they can not be compared quantitatively with previous data because of the different assay conditions. Phosphoglyceromutase in Peaks I, II and III Thermal Inactivation.…”

Section: Enzymic Properties Of Peak IIIsupporting

confidence: 87%

“…Apparent K, f o r 2,3-Bisphosphoglycerate. Rose has reported that the phosphoglyceromutase activity in the purified bisphosphoglyceromutase preparation is enhanced by the addition of a high level of 2,3-bisphosphoglycerate, within which range the main phosphoglyceromutase in red cells is not affected [9]. To examine this with our preparations, kinetic studies on phosphoglyceromutases of three peaks were carried out.…”

Section: Enzymic Properties Of Peak IIImentioning

confidence: 94%

“…Several compounds have been found to have effects on bisphosphoglyceromutase and 2,3-bisphosphoglycerate phosphatase [6,7,9,22]. Effects of these compounds were tested on the two activities of peak I11 (Table 2).…”

Section: Enzymic Properties Of Peak IIImentioning

confidence: 99%

“…The bisphosphoglyceromutase preparation purified by Rose [9], which showed a single protein band on electrophoresis in a polyacrylamide gel containing sodium dodecyl sulphate, had not only phosphoglyceromutase activity but also 2,3-bisphosphoglycerate phosphatase activity in the presence of 2-phosphoglycolate which was a potent activator of the phosphatase [7]. Rosa et al have shown with haemolysates from human and several animal species that bisphosphoglyceromutase and 2,3-bisphosphoglycerate phosphatase are not separable electrophoretically on a starch gel [ll].…”

mentioning

confidence: 99%

“…They also found a human subject who had a partial and equal deficiency of both bisphosphoglyceromutase and 2,3-bisphosphoglycerate phosphatase activities in his erythrocytes [ll]. Although data suggesting a resemblance in the enzymic and physical properties of bisphosphoglyceromutase, 2,3-bisphosphoglycerate phosphatase and phosphoglyceromutase have been accumulated [7,9], it is not yet known whether or not the three activities are really exhibited by a common enzyme protein.…”

mentioning

confidence: 99%

See 4 more Smart Citations

Purification of Bisphosphoglyceromutase, 2, 3-Bisphosphoglycerate Phosphatase and Phosphoglyceromutase from Human Erythrocytes. Three Enzyme Activities in One Protein

et al. 1975

View full text Add to dashboard Cite

Bisphosphoglyceromutase, 2,3-bisphosphoglycerate phosphatase and phosphoglyceromutase have been purified from human red cells. Three enzymes were co-purified throughout all purification steps. Three fractions (peaks 1, I1 and 111) which were chromatographically separable and had three activities in different ratios were obtained.Peak I11 which contained the main bisphosphoglyceromutase and 2,3-bisphosphoglycerate phosphatase activities was purified to homogeneity by electrophoretic and ultracentrifugal analyses. The homogeneous preparation had the phosphoglyceromutase activity. The three activities were lost at the same rate during thermal inactivation. Thus, bisphosphoglyceromutase and 2,3-bisphosphoglycerate phosphatase activities, which are responsible for 2,3-bisphosphoglycerate metabolism in red cells, are displayed by the same enzyme protein which has phosphoglyceromutase activity.Peaks I and 11 were rich in the phosphoglyceromutase activity. Both peaks showed bisphosphoglyceromutase and 2,3-bisphosphoglycerate phosphatase activities, although these two activities were much smaller than those of peak 111.Some of the enzymic properties of peak I11 are described. Comparative studies on three peaks showed that the phosphoglyceromutase of peak111 differed from that of peaks1 and I1 in the kinetic property and thermostability.

show abstract

Section: Enzymic Properties Of Peak IIIsupporting

confidence: 87%

Section: Enzymic Properties Of Peak IIImentioning

confidence: 94%

Section: Enzymic Properties Of Peak IIImentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Purification of Bisphosphoglyceromutase, 2, 3-Bisphosphoglycerate Phosphatase and Phosphoglyceromutase from Human Erythrocytes. Three Enzyme Activities in One Protein

et al. 1975

View full text Add to dashboard Cite

show abstract

An enzyme-linked immunosorbent assay and reference ranges for bisphosphoglycerate mutase in human erythrocytes

Takubo

Izumi

Tatsumi

et al. 1998

J. Clin. Lab. Anal.

View full text Add to dashboard Cite

We established an enzyme-linked immunosorbent assay (ELISA) system for the determination of human bisphosphoglycerate mutase (BPGM) protein content in human erythrocytes using a polyclonal anti-BPGM antibody, we determined reference ranges for BPGM protein content, synthase activity, and specific activity in human erythrocytes. We produced a recombinant human BPGM (rBPGM) by gene manipulation using E. coli and then obtained the polyclonal antibody by immunizing rabbits with purified rBPGM. The reproducibility of the ELISA was in an acceptable range with a coefficient of variation under 1.5%. The ELISA was reliable in the range of 0.1 to 10 ng/mL. The polyclonal anti-rBPGM antibody did not show any cross-reaction with recombinant human B type phosphoglycerate mutase, which is highly homologous to rBPGM. The ELISA was found to be practical for the determination of BPGM protein content in human erythrocytes. The mean BPGM protein content was 56.3 ± 9.7 µg/mL in whole blood (mean ± SD, n = 50). The ELISA can be used to examine various hematologic disorders with abnormal red cell size and cell counts, and to detect BPGM enzymopathy in human erythrocytes.

show abstract

The Enzymology of 2, 3‐Bisphosphoglycerate

Rose

1980

Advances in Enzymology - And Related Areas of Molecular Biology

Self Cite

View full text Add to dashboard Cite

Effects of salts and pH on the rate of erythrocyte diphosphoglycerate mutase

Cited by 44 publications

References 26 publications

Purification of Bisphosphoglyceromutase, 2, 3-Bisphosphoglycerate Phosphatase and Phosphoglyceromutase from Human Erythrocytes. Three Enzyme Activities in One Protein

Purification of Bisphosphoglyceromutase, 2, 3-Bisphosphoglycerate Phosphatase and Phosphoglyceromutase from Human Erythrocytes. Three Enzyme Activities in One Protein

An enzyme-linked immunosorbent assay and reference ranges for bisphosphoglycerate mutase in human erythrocytes

The Enzymology of 2, 3‐Bisphosphoglycerate

Contact Info

Product

Resources

About