-transparent.png){kind=logo}
Previous reports have suggested the possibility of extensive structural homology between human erythrocyte bisphosphoglycerate synthase (glycerate-1,3-P2 leads to glycerate-2,3-P2) and phosphoglycerate mutase (glycerate-3-P in equilibrium glycerate-2-P). This study lends credence to that conjecture through comparative physicochemical investigations involving peptide mapping, circular dichroism, and immunological techniques. The data indicate that despite differences in function, both enzymes apparently manifest a high degree of similarity in primary, secondary, and tertiary structure. Mapping data also indicate that each protein is comprised of two apparently identical subunits.
L F Hass, and
W K Kappel, and
K B Miller, and
R L Engle
June 1985,
Biochemical and biophysical research communications,
L F Hass, and
W K Kappel, and
K B Miller, and
R L Engle
June 1978,
The Journal of biological chemistry,
L F Hass, and
W K Kappel, and
K B Miller, and
R L Engle
September 1979,
The Journal of biological chemistry,
L F Hass, and
W K Kappel, and
K B Miller, and
R L Engle
December 1987,
The Journal of biological chemistry,
L F Hass, and
W K Kappel, and
K B Miller, and
R L Engle
August 1978,
Biochemical and biophysical research communications,
L F Hass, and
W K Kappel, and
K B Miller, and
R L Engle
March 2000,
European journal of biochemistry,
L F Hass, and
W K Kappel, and
K B Miller, and
R L Engle
January 1982,
Methods in enzymology,
L F Hass, and
W K Kappel, and
K B Miller, and
R L Engle
January 1987,
Comparative biochemistry and physiology. B, Comparative biochemistry,
L F Hass, and
W K Kappel, and
K B Miller, and
R L Engle
January 2004,
Hormone research,
L F Hass, and
W K Kappel, and
K B Miller, and
R L Engle
August 1976,
The Journal of biological chemistry,
