[Physicochemical parameters of the surface of bacteria and the penicillin-binding capacity in relation to the sensitivity to penicillins and streptomycin].
Development of resistance to penicillins and streptomycin in bacteria results in an increase in the electrokinetic potential changes in the hydratation rate and isoelectric levels of pH. Changes in the physico-chemical properties of the surface of penicillin-resistant Escherichia depends mainly on the accompanying dissociation. The ability of Escherichia to bind labeled benzylpenicillin is shown. Binding of 35S-benzylpenicillin by Escherichia in S-form correlates with sensitivity of the culture to the antibiotic. The penicillin-resistant mutants in R-form bound the antibiotic to a greater extent than sensitive R-cultures. The role of penicillinase in binding 35S-benzylpenicillin by Escherichia was not shown experimentally. Only increased synthesis of the enzyme by the penicillin-resistant mutants was observed. The ability of Escherichia to bind 35S-benzylpenicillin does not depend on the physico-chemical properties of the cell surface and dissociation.
D018407:Bacterial Physiological Phenomena; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004789:Enzyme Activation / Q000187:drug effects; D004925:Escherichia / Q000187:drug effects; D007526:Isoelectric Point; D008826:Microbial Sensitivity Tests; D009154:Mutation / Q000187:drug effects; D010400:Penicillin G / Q000378:metabolism*; D010403:Penicillin Resistance; D010405:Penicillinase / Q000378:metabolism; D013210:Staphylococcus / Q000187:drug effects; D013307:Streptomycin / Q000037:antagonists & inhibitors*; D013499:Surface Properties
D010405:Penicillinase; D010400:Penicillin G; D013307:Streptomycin
Fiziko-khimicheskie parametry poverkhnosti bakteriĭ i sposobnost' sviazyvat' penitsillin v svianzi s chuvstvitel'nost'iu k penitsillinam i streptomitsinu