Proteins found in the outer membrane of a double membrane that allow permeability in most small molecules.
[G. poros, passageway, + -in]
References in periodicals archive ?
Deletion of the porins MspA and MspC raised the resistance to [beta]-lactam antibiotics without changing its [beta]-lactamase activity.
sup][2],[3] In recent studies, the clinical isolates of this species has not only shown the extended-spectrum [sz]-lactamase TEM-24, which results in resistance to [sz]-lactam antibiotics, [sup][4],[5],[6] but also resistance to quinolones, tetracycline, and chloramphenicol, due to reduced drug uptake, by losing porins on the outer membrane.
Creative Biolabs has successfully expressed different types of membrane proteins such as GPCRs, ion channels, porins, viral proteins, transporters, drug receptors, etc.
In order to get inside the cell, these molecules must pass through porins, which are protein channels that span the outer membrane.
To the Editor: Class 2 and class 3 porin (PorB) proteins are the major proteins found in the outer membrane of Neisseria meningitidis (1); they function as porins, allowing the passage of small molecules through the outer membrane.
2,3] This is accomplished by mutations of genes encoding the outer-membrane protein channels called porins.
These proteins, called porins, are usually employed by bacteria to form channels that allow nutrients to enter through the cell wall.
The analysis of the outer membrane proteins profile by SDS-PAGE showed that both isolates lost the major porins OmpK35 and OmpK36.
coli control strains expressing porins OmpC or OmpF (13).
Unfortunately, we have not investigated porins in our isolate.
AmpC [beta]-lactamase, altered porins, or both are usually responsible for cefoxitin resistance in Escherichia coil We examined the relative importance of each.