Abstract

The relationship of structure to function of glycoproteins from various sources will be studied. The main program will concern glycoproteins whose function involves effects of the physical state of water, the antifreeze glycoproteins from the blood of polar ice fish. Some studies will cover the ovomucin from avian egg whites and yolk membranes. Physical measurements will include such determinations as shape, size, diffusion, viscosity and osmotic pressure. Methods will include analytical ultracentrifugation, laser quasi-elastic light scattering, Raman spectroscopy, nuclear magnetic resonance, electrophoresis, circular dichroism, optical rotatory dispersion, osmometry, viscosimetry and calorimetry. Chemical methods will include structure determinations and chemical derivatizations of protein structure. The above studies and methods will be correlated with studies on the functioning of the proteins and mechanisms whereby these functions work. With the antifreeze glycoproteins, the studies will be directed at the mechanism whereby the freezing temperature of water is anomalously lowered. With the ovomucin, the studies will be on its viscosity characteristics.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM023817-21
Application #
3271863
Study Section
Physiological Chemistry Study Section (PC)
Project Start
1977-06-01
Project End
1986-05-31
Budget Start
1985-06-01
Budget End
1986-05-31
Support Year
21
Fiscal Year
1985
Total Cost
Indirect Cost

  Institution

Name
University of California Davis
Department
Type
Earth Sciences/Resources
DUNS #
094878337
City
Davis
State
CA
Country
United States
Zip Code
95618

  Publications

Means, G E; Feeney, R E (1990) Chemical modifications of proteins: history and applications. Bioconjug Chem 1:2-12
Osuga, D T; Feather, M S; Shah, M J et al. (1989) Modification of galactose and N-acetylgalactosamine residues by oxidation of C-6 hydroxyls to the aldehydes followed by reductive amination: model systems and antifreeze glycoproteins. J Protein Chem 8:519-28
Feeney, R E; Osuga, D T (1988) Egg-white and blood-serum proteins functioning by noncovalent interactions: studies by chemical modification and comparative biochemistry. J Protein Chem 7:667-87
Feeney, R E (1988) Reflections on chemical modification of proteinases and their protein inhibitors. Biochimie 70:1171-7
Penner, M H; Osuga, D T; Meares, C F et al. (1987) The interaction of anions with native and phenylglyoxal-modified human serum transferrin. Arch Biochem Biophys 252:7-14
Feeney, R E (1987) Chemical modification of proteins: comments and perspectives. Int J Pept Protein Res 29:145-61
Bush, C A; Feeney, R E (1986) Conformation of the glycotripeptide repeating unit of antifreeze glycoprotein of polar fish as determined from the fully assigned proton n.m.r. spectrum. Int J Pept Protein Res 28:386-97
Feeney, R E; Burcham, T S; Yeh, Y (1986) Antifreeze glycoproteins from polar fish blood. Annu Rev Biophys Biophys Chem 15:59-78
Burcham, T S; Osuga, D T; Rao, B N et al. (1986) Purification and primary sequences of the major arginine-containing antifreeze glycopeptides from the fish Eleginus gracilis. J Biol Chem 261:6384-9
Burcham, T S; Osuga, D T; Yeh, Y et al. (1986) A kinetic description of antifreeze glycoprotein activity. J Biol Chem 261:6390-7

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