PubMed · 4584506
The source did not provide an abstract. Follow the original record for more information.
Explore connections, maps & timelines
C C Stewart. 1973. Nutrient utilization by peritoneal exudate cells.. https://pubmed.ncbi.nlm.nih.gov/4584506/
Cite the original work for its findings. Save a collection to share your selection of sources.
KEEP EXPLORING
Amino acid (AA) profiles from body fluids such as blood and urine are clinical indicators for diagnosing metabolic and hepatic diseases. Current quantitative methods, such as liquid chromatography-mass spectrometry (LC-MS) with isotopically labelled internal standards (ISs), are costly and technically demanding. This study proposes a cost-efficient alternative using structural isomers as ISs in a direct liquid infusion (DLI) tandem mass spectrometry (MS/MS) approach. The method leverages chimeric spectra and fragment intensity ratios to quantify AAs, demonstrating high linearity and precision even with a 3D ion trap mass analyser. This approach offers a viable strategy for AA quantification in preventive medicine, particularly for screening metabolic diseases such as phenylketonuria, diabetes, and liver dysfunction.
Parasitic protozoa of the genus Leishmania secrete a filamentous macromolecule that forms networks and appears to be associated with cell aggregation. We report here the purification of this parasite antigen from Leishmania major culture supernatant and its compositional (75.6% carbohydrate, 20% phosphate, 4.4% amino acids, w/w), structural, and ultrastructural characterization as a highly unusual proteophosphoglycan (PPG). Mild acid hydrolysis, which cleaves preferentially hexose 1-phosphate bonds, releases the PPG glycans. Their structures are Galbeta1-4Man, Manalpha1-2Man, Galbeta1-3Galbeta1-4Man, PO4-6(Galbeta1-3)0-2Galbeta1-4Man, and PO4-6(Arabeta1-2Galbeta1-3)Galbeta1-4Man. These glycans are also components of the parasite glycolipid lipophosphoglycan, but their relative abundance and structural organization in PPG are different. Some of them represent novel forms of protein glycosylation. 31P NMR on native PPG demonstrates that phosphate is exclusively in phosphodiester bonds and that the basic structure R-Manalpha1-PO4-6-Gal-R connects the glycans. A phosphodiester linkage to phosphoserine (most likely R-Manalpha1-PO4-Ser) anchors the PPG oligosaccharides to the polypeptide. PPG has a unique amino acid composition; glycosylated phosphoserine (>43 mol %), serine, alanine, and proline account for more than 87 mol % and appear to be clustered in large proteinase-resistant domains. Electron microscopy of purified PPG reveals cable-like, flexible, long (to 6 microm), and unbranched filaments. The overall structure of PPG shows many similarities to mammalian mucins. Potential functions of this novel mucin-like molecule for the parasites are discussed.
Several 1,2,3,4-tetrahydroisoquinoline-3-carboxylic acids were synthesized and found to have a transiently increasing effect on the locomotor activity of mice after peripheral injection. Three of the active compounds were detected in the brain after intraperitoneal administration. Two of them, the 7-hydroxy and 7-hydroxy-6-methoxy derivatives, were found as endogenous compounds in untreated rat brain and may play a physiological role. The effects of some of these compounds on the level of various endogenous amines, amino acids and metabolites were examined.