Three ongoing projects are described in this continuation application: 1) ANTIBODY PROJECT: Ring-shaped complexes formed between antibody molecules and bivalent hapten are employed to study the mechanism of complement activation. Electron micrographs of Clr2Cls2 have been obtained, and we are examining the structure of this molecule and its possible mode of interaction with the ring-shaped antibody complexes. 2) CHROMATIN PROJECT: The stability of nucleosomes to extremes of ionic strength and pH is being examined. We find that there is a release of DNA from the nucleosome above pH 9.5. We are measuring the titration behavior of nucleosomes over the entire pH range but especially on the alkaline side where release of DNA occurs. Also, we are studying the salt-induced transfer of nucleosomes between various DNA, and propose to examine that which occurs between procaryotic and eucaryotic DNA. 3) LIPOPROTEIN PROJECT: We are studying triglyceride-rich lipoproteins which have an elevated content of saturated triglycerides. These VLDL exhibit a phase transition at approximately 50 degrees C where the saturated triglycerides melt. We believe that they exist in a fluid but supersaturated state in serum, and that they freeze when isolated at room temperature.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM013914-21
Application #
3268556
Study Section
Biophysics and Biophysical Chemistry B Study Section (BBCB)
Project Start
1976-09-01
Project End
1986-08-31
Budget Start
1985-09-01
Budget End
1986-08-31
Support Year
21
Fiscal Year
1985
Total Cost
Indirect Cost
Name
University of California Los Angeles
Department
Type
Schools of Arts and Sciences
DUNS #
119132785
City
Los Angeles
State
CA
Country
United States
Zip Code
90095
Schumaker, V N; Phillips, M L; Chatterton, J E (1994) Apolipoprotein B and low-density lipoprotein structure: implications for biosynthesis of triglyceride-rich lipoproteins. Adv Protein Chem 45:205-48
Phillips, M L; Tao, M H; Morrison, S L et al. (1994) Human/mouse chimeric monoclonal antibodies with human IgG1, IgG2, IgG3 and IgG4 constant domains: electron microscopic and hydrodynamic characterization. Mol Immunol 31:1201-10
Phillips, M L; Lembertas, A V; Schumaker, V N et al. (1993) Physical properties of recombinant apolipoprotein(a) and its association with LDL to form an LP(a)-like complex. Biochemistry 32:3722-8
Schumaker, V N; Phillips, M L; Hanson, D C (1991) Dynamic aspects of antibody structure. Mol Immunol 28:1347-60
Poon, P H; Schumaker, V N (1991) Measurement of macromolecular interactions between complement subcomponents C1q, C1r, C1s, and immunoglobulin IgM by sedimentation analysis using the analytical ultracentrifuge. J Biol Chem 266:5723-7
Chatterton, J E; Phillips, M L; Curtiss, L K et al. (1991) Mapping apolipoprotein B on the low density lipoprotein surface by immunoelectron microscopy. J Biol Chem 266:5955-62
Lane, P D; Schumaker, V N; Tseng, Y et al. (1991) Isolation of human complement subcomponents C1r and C1s in their unactivated, proenzyme forms. J Immunol Methods 141:219-26
Phillips, M L; Oi, V T; Schumaker, V N (1990) Electron microscopic study of ring-shaped, bivalent hapten, bivalent antidansyl monoclonal antibody complexes with identical variable domains but IgG1, IgG2a and IgG2b constant domains. Mol Immunol 27:181-90
Phillips, M L; Schumaker, V N (1989) Conformation of apolipoprotein B after lipid extraction of low density lipoproteins attached to an electron microscope grid. J Lipid Res 30:415-22
Schumaker, V N; Tseng, Y; Poon, P H et al. (1989) Spontaneous activation of reconstituted and serum C1 and the role of C1-inhibitor. Behring Inst Mitt :102-10

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