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Peptidoglycan,PG ELISA Kit

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Peptidoglycan,PG ELISA Kit For research use only. Not for use in diagnostic procedures.For general protocol and instruction, please click the following links:Quantitative Elisa Kit InstructionSandwich ELISA kit general instruction Competition

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Peptidoglycan,PG ELISA Kit

Peptidoglycan,PG ELISA Kit For research use only. Not for use in diagnostic procedures.For general protocol and instruction, please click the following links:Quantitative Elisa Kit InstructionSandwich ELISA kit general instruction Competition

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$559.00

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Detection Range: 15.6 ng/ml - 1000 ng/ml

Target Introduction:

Peptidoglycan(murein) is a polymer consisting of sugars and amino acids that forms a mesh-like layer outside the plasma membrane of most bacteria, forming the cell wall. The sugar component consists of alternating residues of β-(1,4) linked N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM). Attached to the N-acetylmuramic acid is a peptide chain of three to five amino acids. The peptide chain can be cross-linked to the peptide chain of another strand forming the 3D mesh-like layer. Peptidoglycan serves a structural role in the bacterial cell wall, giving structural strength, as well as counteracting the osmotic pressure of the cytoplasm. Peptidoglycan is also involved in binary fission during bacterial cell reproduction.

The peptidoglycan layer is substantially thicker in Gram-positive bacteria (20 to 80 nanometers) than in Gram-negative bacteria (7 to 8 nanometers). Peptidoglycan forms around 90% of the dry weight of Gram-positive bacteria but only 10% of Gram-negative strains. Thus, presence of high levels of peptidoglycan is the primary determinant of the characterisation of bacteria as Gram-positive. In Gram-positive strains, it is important in attachment roles and serotyping purposes. For both Gram-positive and Gram-negative bacteria, particles of approximately 2 nm can pass through the peptidoglycan.

Some antibacterial drugs such as penicillin interfere with the production of peptidoglycan by binding to bacterial enzymes known as penicillin-binding proteins or DD-transpeptidases. Penicillin-binding proteins form the bonds between oligopeptide crosslinks in peptidoglycan. For a bacterial cell to reproduce through binary fission, more than a million peptidoglycan subunits (NAM-NAG+oligopeptide) must be attached to existing subunits. Mutations in genes coding for transpeptidases that lead to reduced interactions with an antibiotic are a significant source of emerging antibiotic resistance.

Lysozyme, which is found in tears and constitutes part of the body's innate immune system exerts its antibacterial effect by breaking the β-(1,4)-glycosidic bonds in peptidoglycan.

Target Structure:

The peptidoglycan layer in the bacterial cell wall is a crystal lattice structure formed from linear chains of two alternating amino sugars, namely N-acetylglucosamine (GlcNAc or NAGA) and N-acetylmuramic acid (MurNAc or NAMA). The alternating sugars are connected by a β-(1,4)-glycosidic bond. Each MurNAc is attached to a short (4- to 5-residue) amino acid chain, containing L-alanine, D-glutamic acid, meso-diaminopimelic acid, and D-alanine in the case of Escherichia coli (a Gram-negative bacterium) or L-alanine, D-glutamine, L-lysine, and D-alanine with a 5-glycine interbridge between tetrapeptides in the case of Staphylococcus aureus (a Gram-positive bacterium). Peptidoglycan is one of the most important sources of D-amino acids in nature.

Citation:

Growth optimization of Lactobacillus rhamnosus FTDC 8313 and the production of putative dermal bioactives in the presence of manganese and magnesium ions.

http://www.ncbi.nlm.nih.gov/pubmed/23082775

Lew LC, Liong MT, Gan CY

J Appl Microbiol. 2013 Feb;114(2):526-35