Abstract

The ultimate goal of this research is to understand in molecular detail the interactions involved between the enzyme galactosyl transferase and the """"""""modifier"""""""" protein Alpha-lactalbumin. Since general glycosyl transfer by this enzyme occurs in both male and female species in other organs, it is an important example of biological regulation when Alpha-lactalbumin is secreted only in lactating mammary gland to alter the specificity of the system specifically for lactose synthesis. The goals of this current project are to (1) characterize, assign, and map specific cation binding and other regions on the Alpha-lactalbumin moledule in solution, (2) to characterize, describe, and map the substrate (UDPgal) donor site, metal site(s) and (carbohydrate) acceptor site on galactosyl transferase; and (3) to describe the residues and interactions involved in the Alpha-lactalbumin-galactosyl transferase (""""""""lactose synthase"""""""") comples, i.e., the role of Alpha-lactalbumin in lactose biosynthesis. These studies will involve ESR, NMR, photo CIDNP NMR, and fluorescene techniques as well as direct chemical and enzymological approaches.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
Eunice Kennedy Shriver National Institute of Child Health & Human Development (NICHD)
Type
Research Project (R01)
Project #
5R01HD017270-03
Application #
3314279
Study Section
Biophysics and Biophysical Chemistry B Study Section (BBCB)
Project Start
1983-02-01
Project End
1987-01-31
Budget Start
1985-02-01
Budget End
1986-01-31
Support Year
3
Fiscal Year
1985
Total Cost
Indirect Cost

  Institution

Name
Ohio State University
Department
Type
Schools of Arts and Sciences
DUNS #
098987217
City
Columbus
State
OH
Country
United States
Zip Code
43210

  Publications

Berliner, L J; Kaptein, R; Koga, K et al. (1990) NMR studies of the structure and environment of the milk protein alpha-lactalbumin. Basic Life Sci 56:231-53
Maliarik, M; Plessas, N R; Goldstein, I J et al. (1989) ESR and fluorescence studies on the adenine binding site of lectins using a spin-labeled analogue. Biochemistry 28:912-7
Musci, G; Koga, K; Berliner, L J (1988) Methionine-90-spin-labeled bovine alpha-lactalbumin: electron spin resonance and NMR distance measurements. Biochemistry 27:1260-5
Berliner, L J; Koga, K; Nishikawa, H et al. (1987) High-resolution proton and laser photochemically induced dynamic nuclear polarization NMR studies of cation binding to bovine alpha-lactalbumin. Biochemistry 26:5769-74
Permyakov, E A; Murakami, K; Berliner, L J (1987) On experimental artifacts in the use of metal ion chelators for the determination of the cation binding constants of alpha-lactalbumin. A reply. J Biol Chem 262:3196-8
Berliner, L J; Koga, K (1987) Alpha-lactalbumin binding to membranes: evidence for a partially buried protein. Biochemistry 26:3006-9
Musci, G; Berliner, L J (1986) Intramolecular distance measurements in alpha-lactalbumin. Biochemistry 25:4887-91
Musci, G; Reed, G H; Berliner, L J (1986) An electron paramagnetic resonance study of bovine alpha-lactalbumin-metal ion complexes. J Inorg Biochem 26:229-36
Berliner, L J; Musci, G; Maliarik, M et al. (1986) Binding of N-acetylgalactosamine-specific lectins to spin-labeled galactosamine derivatives. Biochemistry 25:4457-61
Musci, G; Berliner, L J (1985) Probing different conformational states of bovine alpha-lactalbumin: fluorescence studies with 4,4'-bis[1-(phenylamino)-8-naphthalenesulfonate]. Biochemistry 24:3852-6

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