Biography:

In the past Kathleen L. Hefferon has collaborated on articles with John W. Hudson. One of their most recent publications is Regular paperComparative analysis of species-independent, isozyme-specific amino-acid substitutions in mammalian muscle, brain and liver glycogen phosphorylases. Which was published in journal Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology.

More information about Kathleen L. Hefferon research including statistics on their citations can be found on their Copernicus Academic profile page.

Kathleen L. Hefferon's Articles: (3)

Regular paperComparative analysis of species-independent, isozyme-specific amino-acid substitutions in mammalian muscle, brain and liver glycogen phosphorylases

AbstractMammalian glycogen phosphorylases exist as three isozymes, muscle, brain and liver, that exhibit different responses to activation by phosphorylation and AMP, regardless of species. To identify species-independent, amino-acid substitutions that may be important determinants in differential isozyme control, we have sequenced cDNAs containing the entire protein coding regions of rat muscle and brain phosphorylases. Nucleotide sequence comparisons with rat liver, rabbit muscle, and human muscle, brain and liver phosphorylase genes, indicate that muscle and brain isozymes are more related to each other than to the liver isozyme. Unlike the human isozymes, there is little difference in GC content of codons in the rat isozymes. In relation to the rabbit muscle isozyme three-dimensional structure, amino-acid sequence comparisons indicate that very few nonconservative isozyme-specific substitutions occur in buried and dimer contact residues. There is strict conservation of active site, pyridoxal-phosphate-binding site and nucleoside inhibitor site residues, as well as CAP loop and helix-2 residues that comprise the phosphorylation activation and part of the AMP binding sites. In contrast, five liver isozyme-specific substitutions occur between residues 313–325 and another at residue 78 which may be important determinants in the poor activation of this isozyme by AMP. Substitutions in the brain isozyme at residues 21–23, 405 and 435 may play a role in its poor response to activation by phosphorylation.

Chapter 16 - Crops With Improved Nutritional Content Though Agricultural Biotechnology

AbstractMalnutrition, resulting from micronutrient deficiencies such as vitamin A, folate, and iron, is and will continue to be, one of the greatest challenges of our world for the next century. One way to address this challenge is the development of food crops through the use of agricultural biotechnology that are rich in vitamins and minerals. The following chapter explores the use of genetic engineering strategies, including transgenesis, RNA interference, and genome editing to create the next generation of biotech crops that can improve the nutritional status of the rural poor in developing countries. The chapter provides a series of examples of crops that have been biofortified through biotechnology, including rice, banana, potato, cassava, and sorghum. Nutritionally enhanced food crops, including tomato, false flax, and Brassica species are also discussed. The chapter ends with a discussion of the potential of biotechnology to provide a more nutritionally secure world.

Expression of a vaccine protein in a plant cell line using a geminivirus-based replicon system

AbstractEdible vaccines have been generated from both transgenic plants as well as from plant viral vectors. Here, we have taken the best attributions of both systems and designed a minimalized version of the bean yellow dwarf geminivirus (BeYDV)-based replicon consisting of the cis-acting elements required for BeYDV replication as a means to express foreign genes in a plant cell line. Replication can be switched on at high levels upon expression of the BeYDV Rep protein, and gene expression enhanced enormously. Construction of an expression cassette encoding a synthetic vaccine gene and analysis of expression levels of a vaccine protein in a plant cell line system are described.

Advertisement
Join Copernicus Academic and get access to over 12 million papers authored by 7+ million academics.
Join for free!

Contact us