Abstract

The ultimate objective of the proposed research is the complete determination of the amino acid sequences of the polypeptide chains of the hemocyanin of Limulus polyphemus. This molecule is a large aggregate of 3.3 x 10 to the 6th power daltons which is composed of 48 subunits each of about 70,000 daltons. As such it constitutes an important model system for the study of self assembly. The subunits are of 8 immunologically distinct types that can be isolated as 5 distinct fractions, each of which is necessary for the assembly of the intact molecule. A prerequisite for complete understanding of the structure and its functional properties is the determination of the primary structure. Our first immediate goal is the determination of the sequence of component II which is being analyzed by x-ray crystallography in another laboratory.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM028410-05
Application #
3275721
Study Section
Physical Biochemistry Study Section (PB)
Project Start
1981-01-01
Project End
1985-12-31
Budget Start
1985-01-01
Budget End
1985-12-31
Support Year
5
Fiscal Year
1985
Total Cost
Indirect Cost

  Institution

Name
University of Texas Austin
Department
Type
Schools of Arts and Sciences
DUNS #
City
Austin
State
TX
Country
United States
Zip Code
78713

  Publications

Pascual, Florencia; Carman, George M (2013) Phosphatidate phosphatase, a key regulator of lipid homeostasis. Biochim Biophys Acta 1831:514-22
Suzuki, T; Riggs, A F (1993) Linker chain L1 of earthworm hemoglobin. Structure of gene and protein: homology with low density lipoprotein receptor. J Biol Chem 268:13548-55
Fushitani, K; Riggs, A F (1991) The extracellular hemoglobin of the earthworm, Lumbricus terrestris. Oxygenation properties of isolated chains, trimer, and a reassociated product. J Biol Chem 266:10275-81
Jhiang, S M; Garey, J R; Riggs, A F (1988) Exon-intron organization in genes of earthworm and vertebrate globins. Science 240:334-6
Fushitani, K; Matsuura, M S; Riggs, A F (1988) The amino acid sequences of chains a, b, and c that form the trimer subunit of the extracellular hemoglobin from Lumbricus terrestris. J Biol Chem 263:6502-17
Fushitani, K; Riggs, A F (1988) Non-heme protein in the giant extracellular hemoglobin of the earthworm Lumbricus terrestris. Proc Natl Acad Sci U S A 85:9461-3
Garey, J R; Riggs, A F (1986) The hemoglobin of Urechis caupo. The cDNA-derived amino acid sequence. J Biol Chem 261:16446-50
Nakashima, H; Behrens, P Q; Moore, M D et al. (1986) Structure of hemocyanin II from the horseshoe crab, Limulus polyphemus. Sequences of the overlapping peptides, ordering the CNBr fragments, and the complete amino acid sequence. J Biol Chem 261:10526-33
Behrens, P Q; Nakashima, H; Yokota, E et al. (1986) The structure of hemocyanin II from the horseshoe crab, Limulus polyphemus. The amino acid sequence of the second largest cyanogen bromide fragment. J Biol Chem 261:10520-5
Moore, M D; Behrens, P Q; Riggs, A F (1986) The structure of hemocyanin II from the horseshoe crab, Limulus polyphemus. The amino acid sequences of the smaller cyanogen bromide fragments. J Biol Chem 261:10511-9

Showing the most recent 10 out of 12 publications