D-Amino acids in mammals and their diagnostic value.

��������� � �� ���������� Viral infection of bacteria causes release of dissolved organic matter (DOM), which is available for bacterial uptake. In aquatic environments, this virus-mediated transformation of living cells into dissolved and colloidal organic matter may be a quantitatively important process in the pelagic recycling of carbon and nutrients, but little is known about the amount, composition, or bioavailability of viral lysates. By using a model system of a marine bacterium (Cellulophaga sp.) and a virus speci¢c to this bacterium, the present study provides a ¢rst quanti¢cation of the input of dissolved free and combined amino acids (DFAA and DCAA) and bacterial cell wall compounds following viral lysis. The DCAA constituted 51^86% of the total virus-mediated organic carbon release of 1087^1825m gCl 71 (estimated biomass of the lysed bacteria), whereas DFAA and glucosamine each accounted for 2^3% of total lysate-C. The viral particles themselves constituted 4^6% of the released organic carbon, and altogether, the applied analyses thus identi¢ed 53^92% of the released lysates. Approximately 12% of the identi¢ed compounds were derived from bacterial cell wall peptidoglycan, including various D-isomers of DFAA and DCAA, glucosamine and diaminopimelic acid (DAPA). Although a portion of this cell wall material may have entered the pool of refractory material, a signi¢cant fraction of some peptidoglycan-derived components, e.g. 83% of the released D-DFAA, were removed from the dissolved phase during the last part of the incubations, suggesting that part of the cell wall material were utilized by the developing virus-resistant Cellulophaga population. Therefore, we suggest that virus-mediated DOM is a source of a variety of organic compounds, which contribute signi¢cantly to the pool of rapidly recycling material in the ocean.

/pdf/viral-lysis-of-bacteria-an-important-source-of-dissolved-372tf54stn.pdf

Viral lysis of bacteria: an important source of dissolved amino acids and cell wall compounds

Regional distribution and postnatal changes of d-amino acids in rat brain

Amino acid analysis is used to determine the amino acid content of amino acid-, peptide- and protein-containing samples. With minor exceptions, proteins are long linear polymers of amino acids connected to each other via peptide bonds. The first step of amino acid analysis involves hydrolyzing these peptide bonds. The liberated amino acids are then separated, detected, and quantified. The method was first developed by Moore, Stein and coworkers in the 1950s using HCl acid hydrolysis, and, despite considerable effort by many workers, the basic methodology remains relatively unchanged. This unit provides an overview and strategic planning for amino acid analysis, discussing a range of methodologies and issues. In addition, several common methods used for analysis of L-amino acids are described in detail, including: HCl acid hydrolysis, performic acid oxidation for methionine and cysteine analysis, base hydrolysis for tryptophan analysis, analysis of free amino acids, and analysis of reactive lysine.

Amino Acid Analysis

Immune cells exhibit distinct stereospecific behaviors on enantiomorphous surfaces with different chiralities. It may not only bring interesting insight to the design of novel high-performance biocompatible materials but also help to better understand the high selectivity of chirality in biosystems.

Stereospecific Interaction between Immune Cells and Chiral Surfaces

Liquid chromatographic determination of d- and l-amino acids by derivatization with o-phthaldialdehyde and chiral thiols: Applications with reference to biosciences

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Liquid chromatographic determination of d- and l-amino acids by derivatization with o-phthaldialdehyde and chiral thiols: Applications with reference to biosciences