Evidence map›Paper›PMID 7915268›Full record

ArticleJournal of bacteriology1994

Analysis of the sodium dodecyl sulfate-stable peptidoglycan autolysins of select gram-negative pathogens by using renaturing polyacrylamide gel electrophoresis.

G Bernadsky, T J Beveridge, A J Clarke

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Journal of bacteriology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.4field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

24 citing papers in PubMed, 75 citations in OpenAlex.

  1. Measure of Peptidoglycan Degradation Activity.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  2. Article
  3. Applied and environmental microbiology · 2021
    Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Peptidoglycan hydrolases of Escherichia coli.Microbiology and molecular biology reviews : MMBR · 2011
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

G BernadskyCanadian Bacterial Diseases Network, Department of Microbiology, College of Biological Science, University of Guelph, Ontario.
T J Beveridge
A J Clarke
University of Guelph · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

For the first time, peptidoglycan autolysins from cellular fractions derived from sonicated cultures of Pseudomonas aeruginosa PAO1, Escherichia coli W7, Klebsiella pneumoniae CWK2, and Proteus mirabilis 19 were detected and partially characterized by zymogram analysis. Purified murein sacculi from P. aeruginosa PAO1 were incorporated into a sodium dodecyl sulfate (SDS)-polyacrylamide gel at a concentration of 0.05% (wt/vol) to serve as a substrate for the separated autolysins. At least 11 autolysin bands of various intensities with M(r)s ranging between 17,000 and 122,000 were detected in each of the homogenated cultures. Some of the autolysins of the four bacteria had similar M(r)s. The zymogram analysis was used to show that a number of the autolysins from E. coli were inhibited by the heavy metals Hg2+ and Cu2+, at 1 and 10 mM, respectively, high ionic strengths, and reagents known to affect the packing of lipopolysaccharides. The activity of an autolysin with an M(r) of 65,000 was also impaired by penicillin G, whereas it was enhanced by gentamicin. A preliminary screen to determine the relationship between penicillin-binding proteins (PBPs) and autolysins was carried out by using a dual assay in which radiolabelled penicillin V bands were visualized on an autolysin zymogram. Radiolabelled bands corresponding to PBPs 3, 4, 5, and 6 from E. coli and P. aeruginosa; PBPs 3, 4, and 6 from Proteus mirabilis; and PBP 6 from K. pneumoniae degraded the murein sacculi in the gels and were presumed to have autolytic activity, although the possibility of two distinct enzymes, each with one of the activities, comigrating in the SDS-polyacrylamide gels could not be excluded. Some radiolabelled bands possessed an Mr of <34,000 and coincided with similar low-Mr autolysin bands.

Indexed as

Sodium Dodecyl SulfateCations, DivalentElectrophoresis, Polyacrylamide GelEscherichia coliGram-Negative BacteriaKineticsKlebsiella pneumoniaeMolecular WeightN-Acetylmuramoyl-L-alanine AmidaseProteus mirabilisPseudomonas aeruginosaCations, DivalentN-Acetylmuramoyl-L-alanine AmidaseSodium Dodecyl Sulfate

Identifiers

PMID7915268
PMCPMC196705
OpenAlexW1949381244

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.