1985
DOI: 10.1007/bf02922493
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Purification and characterization of pyocins frompseudomonas aeruginosa

Abstract: Three types of pyocins were found in Pseudomonas aeruginosa strain 986 and named pyocin type P25, P50, and P70. Production of these types was inducible by UV irradiation. Their molar mass was estimated. The pyocins obtained were different from the known pyocins R, S, and F in their chemical and physical properties. No immunological cross reaction was observed among these pyocins.

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Cited by 3 publications
(4 citation statements)
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“…The final purification that was achieved after gel filtration chromatography was 8.2 folds with 2% recovery. These findings are in accordance with another study which also reported the purification of pyocin with an increase in the specific activity as well as purification up to 434-fold ( Al-Shibib et al ., 1985 ). In another study, the specific activity of the pyocin after every step of purification was increased and final recovery after chromatography using Sephacryl S 200 was observed to be 13% ( Sano and Kageyama, 1981 ).…”
Section: Resultssupporting
confidence: 93%
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“…The final purification that was achieved after gel filtration chromatography was 8.2 folds with 2% recovery. These findings are in accordance with another study which also reported the purification of pyocin with an increase in the specific activity as well as purification up to 434-fold ( Al-Shibib et al ., 1985 ). In another study, the specific activity of the pyocin after every step of purification was increased and final recovery after chromatography using Sephacryl S 200 was observed to be 13% ( Sano and Kageyama, 1981 ).…”
Section: Resultssupporting
confidence: 93%
“…In the following step of conventional gel permeation chromatography, on Sephadex G-75 column, pyocin SA189 depicted the activity to reside in fraction 6, 7 and 8 and the chromatogram also showed a single peak of protein ( Figure 2 ). These findings correlate with the study, where pyocin was eluted from the CM Sephadex A-50 (pH 7.2) column as a single protein peak ( Al-Shibib et al ., 1985 ). Furthermore, Duport et al .…”
Section: Resultssupporting
confidence: 90%
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“…Interest in these particles continued to grow in the 1970s and 1980s as more R-pyocins became identified and purified ( Chen and Tai, 1972 ; Garcia Rodriguez and Saenz Gonzalez, 1972 ; Shinomiya, 1972 ; Govan, 1974a ; Al-Shibib et al, 1985 ; Al-Rubiee et al, 1988 ). Some of these R-pyocins were compared with each other and the tail fibers were identified as the component involved in their specificity ( Ohsumi et al, 1980 ; Kumazaki and Ishii, 1982 ).…”
Section: A Brief History Of Ecissmentioning
confidence: 99%