Molecular Sciences Faculty Directory
Lorraine M. Kraus, Ph.D.
Professor Emeritus - Active
894 Union Avenue
Room 105 Nash Building
Memphis, TN 38163
Email: lkraus@utmem.edu
Phone: 901-448-4374
Fax: 901-448-7126
Research Interests
Urea and cyanate, spontaneously transformed from urea, are increased with decreased renal function becoming potential toxins. Isocyanic acid, the active form of cyanate, carbamoylates proteins, amino acids and other molecules in vivo changing molecular function, structure and charge. Carbamoylation can occur at multiple sites with a cumulative effect over the life span of the molecule. A new molecule of cyanate is formed when carbamoylation removes a molecule of cyanate, because of the equilibrium between urea and cyanate. Isocyanic acid reacts irreversibly with the non-protonated a-amino group of amino acids forming carbamoylated amino acids (C-AA) from free amino acids (F-AA). C-AA interfere with protein synthesis and transamination reactions and contribute in part to protein-malnutrition.
The irreversible carbamoylation of the e-amino group of lysine forming e -amino-carbamoyl-lysine (homocitrulline) occurs at multiple sites within a protein changing the site of molecular activity. Reversible carbamoylation occurs at the hydroxyl group of tyrosine, serine, or threonine and the sulfhydryl group of cysteine depending upon the pH of the microinvironment. Carbamoylation can effect the biological activity of enzymes, coenzymes, antibodies, hormones, receptors, and transport proteins. Carbamoyl-molecules can block, enhance or be excluded from metabolic pathways, and can effect binding and trafficking, thereby influencing the fate of non-carbamoylated molecules.
PubMed search for Dr. Lorraine M. Kraus
Education
- B.S. 1943 Mount Mary College, Chemistry/Biology
- Michael Reese Hospital, A.S.C.P., 1943 Medical Technology M.T.
- Memphis Academy of Arts, B.F.A. 1982 Painting and Etching, M.F.A. 1991 Painting
- M.S. 1952 University of Tennessee, Center for the Health Science, Biochemistry
- Ph.D. 1956, University of Tennessee Health Science Center, Biochemistry
