A competitive radioimmunoassay for peptidoglycan monomer.

Clin Chim Acta

Department of Radioimmunology, Institute of Immunology, Zagreb, Croatia, Yugoslavia.

Published: October 1991

The preparation and characterization of the essential components to be used in the radioimmunoassay of peptidoglycan monomer (PGM) is described. In order to raise the anti-peptidoglycan monomer antibodies 14C-labelled peptidoglycan monomer-bovine serum albumin conjugate was prepared by the coupling of 14C-peptidoglycan monomer to bovine serum albumin in the presence of glutaraldehyde in 0.1 M NaHCO3 at pH 8.3. The prepared conjugate elicited anti-PGM response in rabbits. A synthetic analog of peptidoglycan monomer, Boc-L-tyrosyl-peptidoglycan monomer was prepared by condensation of unprotected peptidoglycan monomer and N-hydroxysuccinimidester of Boc-L-tyrosine in the presence of triethylamine and the obtained disaccharide-hexapeptide was labelled with Na125I. This compound exhibited the ability of binding to anti-peptidoglycan monomer antibodies. The prepared compounds, namely anti-PGM antibodies and 125I-labelled Boc-L-tyrosyl-peptidoglycan monomer, were used as essential components in competitive radioimmunoassay for peptidoglycan monomer determination in mammalian and human sera and plasma, respectively.

Download full-text PDF

Source
http://dx.doi.org/10.1016/0009-8981(91)90252-8DOI Listing

Publication Analysis

Top Keywords

peptidoglycan monomer
20
radioimmunoassay peptidoglycan
12
monomer
10
competitive radioimmunoassay
8
essential components
8
anti-peptidoglycan monomer
8
monomer antibodies
8
serum albumin
8
boc-l-tyrosyl-peptidoglycan monomer
8
peptidoglycan
6

Similar Publications

Structural Characterization and Immune Activation Capacity of Peptidoglycan from in RAW264.7 Cells.

Int J Mol Sci

December 2024

Key Laboratory of Feed Biotechnology of the Ministry of Agriculture and Rural Affairs, Risk Assessment Laboratory of Animal Product Quality Safety Feed Source Factors of the Ministry of Agriculture and Rural Affairs, Institute of Feed Research of Chinese Academy of Agricultural Sciences, Beijing 100081, China.

Peptidoglycan (PGN) is a unique component of prokaryotic cell walls with immune-enhancing capacities. Here, we extracted PGN from , a by-product of amino acid fermentation, using the trichloroacetic acid (TCA) method. SDS-PAGE analysis confirmed the presence of PGN, with a band of approximately 28 kDa.

View Article and Find Full Text PDF

Peatlands are invaluable but threatened ecosystems that store huge amounts of organic carbon globally and emit the greenhouse gasses carbon dioxide (CO) and methane (CH). Trophic interactions of microbial groups essential for methanogenesis are poorly understood in such systems, despite their importance. Thus, the present study aimed at unraveling trophic interactions between fermenters and methanogens in a nitrogen-limited, subarctic, pH-neutral fen.

View Article and Find Full Text PDF

Phage-derived peptidoglycan hydrolases (i.e. lysins) are considered promising alternatives to conventional antibiotics due to their direct peptidoglycan degradation activity and low risk of resistance development.

View Article and Find Full Text PDF

is a Gram-positive anaerobic spore-forming bacterial pathogen of humans and animals. also produces type IV pili (T4P) and has two complete sets of T4P-associated genes, one of which has been shown to produce surface pili needed for cell adherence. One hypothesis about the role of the other set of T4P genes is that they could comprise a system analogous to the type II secretion systems (TTSS) found in Gram-negative bacteria, which is used to export folded proteins from the periplasm through the outer membrane to the extracellular environment.

View Article and Find Full Text PDF
Article Synopsis
  • - The peptidoglycan pathway, crucial for bacterial cell wall formation, targets the translocation of undecaprenyl phosphate (C-P) across the membrane, which is facilitated by proteins like DedA and UptA.
  • - Research using native mass spectrometry reveals that UptA binds C-P more effectively than shorter-chain lipid analogs and interacts in a pH-sensitive manner.
  • - The study also finds that certain lipopeptide antibiotics can inhibit UptA by competing for its binding site, suggesting potential directions for developing new antibiotics that target lipid recycling processes in bacteria.
View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!