Abstract

The objectives of this proposal are to understand the principles involved in the metabolic regulation of normal and abnormal erythrocytes. Particular emphasis will be placed on the investigation of those enzymes responsible for the synthesis, degradation, and utilization of glycerate-2,3-P2. The enzymes of special interest are bisphosphoglycerate synthase, phosphoglycerate mutase, and phosphoglycerate kinase. This study will include an evaluation of certain regulatory substances and intracellular environmental conditions which might ameliorate sickle cell anemia, other cardiovascular disorders, and blood storage problems.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Heart, Lung, and Blood Institute (NHLBI)
Type
Research Project (R01)
Project #
5R01HL016647-10
Application #
3335244
Study Section
Biochemistry Study Section (BIO)
Project Start
1976-12-01
Project End
1986-12-31
Budget Start
1985-01-01
Budget End
1985-12-31
Support Year
10
Fiscal Year
1985
Total Cost
Indirect Cost

  Institution

Name
Pennsylvania State University
Department
Type
Schools of Medicine
DUNS #
129348186
City
Hershey
State
PA
Country
United States
Zip Code
17033

  Publications

Stankiewicz, P J; Gresser, M J; Tracey, A S et al. (1987) 2,3-diphosphoglycerate phosphatase activity of phosphoglycerate mutase: stimulation by vanadate and phosphate. Biochemistry 26:1264-9
Smith, G C; McWilliams, A D; Hass, L F (1986) Wheat germ phosphoglycerate mutase: evidence for a metalloenzyme. Biochem Biophys Res Commun 136:336-40
Stankiewicz, P J; Hass, L F (1986) The catalytic bimodality of mammalian phosphoglycerate mutase. J Biol Chem 261:12715-21
Smith, G C; Hass, L F (1985) Wheat germ phosphoglycerate mutase: purification, polymorphism, and inhibition. Biochem Biophys Res Commun 131:743-9