The Modification of Arginine
Roger L. Lundblad, Claudia M. Noyes in Chemical Reagents for Protein Modification, 1984
Until approximately 10 years ago the specific chemical modification of arginine was relatively difficult to achieve. The high pKa of the guanidine functional group necessitated fairly drastic reaction conditions to generate an effective nucleophile. The modification of arginyl residues with glyoxal has also been proposed. Specificity of reaction is a problem with reaction also at primary amine groups and sulfhydryl groups. The determination of the extent of arginine modification is generally determined by amino acid analysis after acid hydrolysis but conditions generally need to be modified to prevent loss of the arginine derivative. Of particular interest has been the observations of Fonda and Cheung that the reaction of arginine with phenylglyoxal is greatly accelerated in bicarbonate-carbonate buffer systems. The ability of 2,3-butanedione to act as a photosensitizing agent for the destruction of amino acids and proteins in the presence of oxygen was emphasized in work by Fliss and Viswanatha.
The parathyroid glands and vitamin D
S.S. Nussey, S.A. Whitehead in Endocrinology, 2001
Multiple symptoms arise when disease leads to hyper-or hypocalcemia and Clinical Case 5.1 illustrates features of hypercalcemia. Clinical Case 5.1 is a middle-aged woman suffering from the consequences of marked hypercalcemia, presenting with symptoms of polydipsia and polyuria. These, together with the weight loss, made her primary care physician suspect DM. However, this patient had anorexia whilst DM is much more commonly associated with a good appetite, despite weight loss. The polyuria resulted from the effects of hypercalcemia antagonizing the action of arginine vasopressin on the distal tubule and collecting ducts of the kidney (see Box 7.42). The resulting diuresis stimulated thirst and led to polydipsia. Her anorexia was due to the effects of hypercalcemia acting on the brain to reduce appetite.
The Modification Of Arginine
Roger L. Lundblad in Chemical Reagents for Protein Modification, 2020
This chapter discusses the reaction of arginyl residues in proteins with three different reagents; phenylglyoxal, 2,3-butanedione, and 1,2-cyclohexanedione since the vast majority of reports during the past decade have used these reagents. The sulfonic acid function provides a basis for the attachment of a “tag” such as norleucine which can be used for determining the extent of modification. The determination of the extent of arginine modification is generally determined by amino acid analysis after acid hydrolysis but conditions generally need to be modified to prevent loss of the arginine derivative. The use of isolated “membrane fraction” prevented the establishment of stoichiometry in the studies. Analysis of the dependence of reaction rate on concentration of 2,3-butanedione is consistent with the modification of a single arginine residue. The ability of 2,3-butanedione to act as a photosensitizing agent for the destruction of amino acids and proteins in the presence of oxygen was emphasized in work by H. Fliss and T. Viswanatha.
Mechanism of
Published in Agricultural and Biological Chemistry, 1979
Hajime Yoshida, Kazumi Araki, Kiyoshi Nakayama
Regulatory properties of the arginine biosynthetic enzymes in the l-arginine producers of Corynebacterium glutamicum were examined. d-Serine-sensitive l-arginine producer, DSS–8, had derepressed level of l-arginine biosynthetic enzymes, but had an N-acetylglutamokinase, the key enzyme of l-arginine biosynthetic pathway, sensitive to the feedback inhibition by l-arginine. d-Serine-sensitive and d-arginine-resistant l-arginine producer, KY10479, had an N-acetylglutamokinase released from the feedback inhibition by l-arginine. Implications of these results are discussed in relation to l-arginine productivity, d-serine sensitivity, l-arginine analog resistance and regulation of l-arginine biosynthesis in these mutants.
Effect of L-arginine and an Arginine-Containing Pentapeptide on Canine Femoral Arterial Blood Flow
Published in Upsala Journal of Medical Sciences, 1991
K. Saldeen, W. W. Nichols, F. Nicolini, J. Mehta
The amino acid L-arginine is a precursor of endothelium derived relaxing factor (EDRF). The pentapeptide 6A (Ala-Arg-Pro-Ala-Lys) released by plasmin degradadation of fibrinogen also contains arginine and relaxes vascular smooth muscle by releasing EDRF (nitric oxide). To determine and compare the effects of L-arginine, peptide 6A and a combination of L-arginine and peptide 6A on femoral artery blood flow and vascular resistance, anesthetized mongrel dog were administered saline, L-arginine, D-arginine, peptide 6A and L-arginine + peptide 6A in a random order. L-arginine and peptide 6A both induced an immediate dose-dependent short-lasting increase in femoral blood flow and a decrease in vascular resistance. Peptide 6A exerted a much greater (P
The effects on plasma L-arginine levels of combined oral L-citrulline and L-arginine supplementation in healthy males
Published in Bioscience, Biotechnology, and Biochemistry, 2017
Takashi Suzuki, Masahiko Morita, Toshio Hayashi, Ayako Kamimura
We investigated the effects of combining 1 g of l-citrulline and 1 g of l-arginine as oral supplementation on plasma l-arginine levels in healthy males. Oral l-citrulline plus l-arginine supplementation more efficiently increased plasma l-arginine levels than 2 g of l-citrulline or l-arginine, suggesting that oral l-citrulline and l-arginine increase plasma l-arginine levels more effectively in humans when combined.