Abstract
The optimum conditions for pigment production by Ae. liquefaciens was found to be 30 °C and aerobic incubation, and the properties of the pigment are shown to be similar to those of the synthetic dopa-melanin referred to. The enzyme phenol oxidase was demonstrated in the culture filtrates, but not in extracts of disintegrated cells. As precursors for the pigment production, which was shown to be strictly pH dependent, DL-tyrosine, DL-dopa and catechol were used with success, while numerous other amino acids failed. The significance of the pigment as a criterium for the identification of strains which are pathogenic to certain animals or fishes, is not known.
Sammendrag
De optimale atmosfære- og temperaturforhold for pigmentproduksjon hos Ae. liquefaciens ble funnet å være aerob inkubasjon ved 30 °G, og pigmentets egenskaper tilsvarer egenskapene til det syntetiske dopamelanin som det refereres til. Enzymet phenoloxidase ble påvist i kulturfiltrat av Ae. liquefaciens, men ikke i ekstrakt av knuste bakterieceller. Som byggesteiner for pigment-produksjonen ble DL-tyrosin, DL-dopa og catechol brukt med suksess, mens flere andre aminosyrer ikke induserte pigmentproduksjonen. Betydningen av pigmentet som kriterium for identifikasjon av stammer som er patogene for enkelte dyr eller fisk er ikke kjent.
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References
- Blackberg S N, Wanger J O. Melanuria. J. Amer. med. Ass. 1933;100:334–336. doi: 10.1001/jama.1933.02740050030009. [DOI] [Google Scholar]
- Carberry, J. T.: Ulcerative dermal necrosis of salmonicids in Ireland. Symp. zool. Soc., London 1968, No. 24, 39–49.
- Cooper J A, Christine Brown F. A rapid semi-quantitative method for the assay of tyrosinase activity. Clin. chim. Acta. 1956;1:301–304. doi: 10.1016/0009-8981(56)90001-8. [DOI] [PubMed] [Google Scholar]
- Dahle H K. Enzymoserological separation of bacterial proteinases. Acta path, microbiol. scand. 1969;76:143–148. doi: 10.1111/j.1699-0463.1969.tb04215.x. [DOI] [PubMed] [Google Scholar]
- Dahle H K. Regulation of the proteinase production in two strains of Aeromonas. Acta path, microbiol. scand. 1971;79:739–746. doi: 10.1111/j.1699-0463.1971.tb00105.x. [DOI] [PubMed] [Google Scholar]
- Fox D L. Animal Biochromes and Structural Colours; Physical, Chemical, Distributional and Physiological Features of Coloured Bodies in the Animal World. London and New York: Cambridge Univ. Press; 1953. [Google Scholar]
- Griffin P J, Snieszko S F, Friddle S B. Pigment formation by Bacterium salmonicida. J. Bact. 1953;65:652–659. doi: 10.1128/JB.65.6.652-659.1953. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Holt G, Hastein T. Furunculosis in fish in Norway. Nord. Vet.- Med. 1970;22:505–509. [Google Scholar]
- Lerner A B, Fitzpatrick T B. Biochemistry of melanin formation. Physiol. Rev. 1950;30:91–126. doi: 10.1152/physrev.1950.30.1.91. [DOI] [PubMed] [Google Scholar]
- Mason H S. Classification of melanins. N.Y. Acad. Sei. Spec. Publ. 1948;4:399–405. [PubMed] [Google Scholar]
- Mason H S. Comparative biochemistry of the phenolase complex. Advanc. Enzymol. 1955;16:105–184. doi: 10.1002/9780470122617.ch3. [DOI] [PubMed] [Google Scholar]
- Masonti S. Structure of melanins. In: M G, editor. Pigment Cell Biology. New York: Acad. Press; 1959. pp. 563–582. [Google Scholar]
- Mencher J R, Heim A H. Melanin biosynthesis by Streptomyces lavendulae. J. gen. Microbiol. 1962;28:665–670. doi: 10.1099/00221287-28-4-665. [DOI] [Google Scholar]
- Meyer F P. Field treatments of Aeromonas liquefaciens in golden strimers. Progve Fish Cult. 1964;26:33–35. doi: 10.1577/1548-8659(1964)26[33:FTOALI]2.0.CO;2. [DOI] [Google Scholar]
- Rock L F, Nelson H M. Charmel catfish and gizzard shad mortality by Aeromonas liquefaciens. Progve Fish Cult. 1965;27:138–141. doi: 10.1577/1548-8640(1965)27[138:CCAGSM]2.0.CO;2. [DOI] [Google Scholar]
- Ross A J. Isolation of a pigment producing strain of Aeromonas liquefaciens from silver salmon (Oncorhynchus kisutch). J. Bact. 1962;84:590–591. doi: 10.1128/JB.84.3.590-591.1962. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Yasunobu K T. Mode of action of tyrosinase. In: M G, editor. Pigment Cell Biology. New York: Acad. Press; 1959. pp. 583–608. [Google Scholar]