Localization of periplasmic redox proteins of Alcaligenes faecalis by a modified general method for fractionating gram-negative bacteria
Journal of Bacteriology, ISSN: 0021-9193, Vol: 181, Issue: 20, Page: 6540-6542
1999
- 12Citations
- 14Captures
Metric Options: CountsSelecting the 1-year or 3-year option will change the metrics count to percentiles, illustrating how an article or review compares to other articles or reviews within the selected time period in the same journal. Selecting the 1-year option compares the metrics against other articles/reviews that were also published in the same calendar year. Selecting the 3-year option compares the metrics against other articles/reviews that were also published in the same calendar year plus the two years prior.
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations12
- Citation Indexes12
- 12
- CrossRef9
- Captures14
- Readers14
- 14
Article Description
A lysozyme-osmotic shock method is described for fractionation of Alcaligenes faecalis which uses glucose to adjust osmotic strength and multiple osmotic shocks. During phenylethylamine-dependent growth, aromatic amine dehydrogenase, azurin, and a single cytochrome c were localized in the periplasm. Their induction patterns are different from those for the related quinoprotein methylamine dehydrogenase and its associated redox proteins.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0032693610&origin=inward; http://dx.doi.org/10.1128/jb.181.20.6540-6542.1999; http://www.ncbi.nlm.nih.gov/pubmed/10515948; https://journals.asm.org/doi/10.1128/JB.181.20.6540-6542.1999; https://dx.doi.org/10.1128/jb.181.20.6540-6542.1999; https://jb.asm.org/content/181/20/6540
American Society for Microbiology
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