scholarly journals Purification and characterization of two killer toxins originated from Torulaspora delbrueckii (Lindner) and Wickerhamomyces anomalus (E.C.Hansen) Kurtzman, Robnett, and Basehoar-Powers

Author(s):  
Najwa Mohammed Jameel Ali Abu-Mejdad ◽  
Adnan I. Al-Badran ◽  
Abdullah H. Al-Saadoon
2014 ◽  
Vol 57 (4) ◽  
pp. 587-594 ◽  
Author(s):  
María Alicia Martos ◽  
Ana Paula Butiuk ◽  
Natalia Lorena Rojas ◽  
Roque Alberto Hours

2014 ◽  
Vol 57 (4) ◽  
pp. 587-594
Author(s):  
María Alicia Martos ◽  
Ana Paula Butiuk ◽  
Natalia Lorena Rojas ◽  
Roque Alberto Hours

2020 ◽  
Vol 44 (1) ◽  
Author(s):  
Najwa Mohammed Jameel Ali Abu-Mejdad ◽  
Adnan I. Al-Badran ◽  
Abdullah H. Al-Saadoon ◽  
Mohammed Hussein Minati

Abstract Background The K1, K2, and K28 toxins are usually encoded by several cytoplasmically genetic satellite dsRNAs (M1, M2, and M28), which are encapsulated with virus-like particles (VLPs) and reliant on an additional assembly of assistant yeast viruses (L-A) for their reproduction and encapsidation. Ascomycetous yeast species that have these VLPs are especially attractive targets for finding killer toxins like proteins. This is because the organisms are known in producing a large variety of secondary metabolites and extracellular enzymes, which have medical importance as alternative drugs for resistance bacterial strains, particularly multi-resistance drugs (MRD). Results For the first time, 31 type strains of yeasts were tested for killer toxin production in Iraq via the measurement of gene expression of three killer toxin genes (M1, M2, and M28) within the mycovirus in yeasts. All the type strains gave an expression for the three killer toxins with variable levels. The highest expression was recorded for the killer toxin genes in Torulaspora delbrueckii followed by Wickerhamomyces anomalus. Determined antibacterial activity of two killer toxins appeared with high inhibition zone against pathogenic strains of bacteria. Cytotoxicity against human blood cells was not found. These results considered the first record of killer toxins isolated from type strains in Iraq. Conclusion The two typical strains Torulaspora delbrueckii and Wickerhamomyces anomalus showed the highest level of gene expression for the three killer toxins.


1994 ◽  
Vol 92 (3) ◽  
pp. 479-486 ◽  
Author(s):  
Cynthia M. Galloway ◽  
W. Mack Dugger

1985 ◽  
Vol 54 (02) ◽  
pp. 485-489 ◽  
Author(s):  
Yukiyoshi Hamaguchi ◽  
Masuichi Ohi ◽  
Yasuo Sakakura ◽  
Yasuro Miyoshi

SummaryTissue-type plasminogen activator (TPA) was purified from maxillary mucosa with chronic inflammation and compared with urokinase. Purification procedure consisted of the extraction from delipidated mucosa with 0.3M potassium acetate buffer (pH 4.2), 66% saturation of ammonium sulfate, zinc chelate-Sepharose, concanavalin A-Sepharose and Sephadex G-100 gel filtration chromatographies.The molecular weight of the TPA was approximately 58,000 ± 3,000. Its activity was enhanced in the presence of fibrin and was quenched by placental urokinase inhibitor, but not quenched by anti-urokinase antibody. The TPA made no precipitin line against anti-urokinase antibody, while urokinase did.All these findings indicate that the TPA in maxillary mucosa with chronic inflammation is immunologically dissimilar to urokinase and in its affinity for fibrin.


1979 ◽  
Author(s):  
M Ribieto ◽  
J Elion ◽  
D Labie ◽  
F Josso

For the purification of the abnormal prothrombin (Pt Metz), advantage has been taken of the existence in the family of three siblings who, being double heterozygotes for Pt Metz and a hypoprothrombinemia, have no normal Pt. Purification procedures included barium citrate adsorption and chromatography on DEAE Sephadex as for normal Pt. As opposed to some other variants (Pt Barcelona and Madrid), Pt Metz elutes as a single symetrical peak. By SDS polyacrylamide gel electrophoresis, this material is homogeneous and appears to have the same molecular weight as normal Pt. Comigration of normal and abnormal Pt in the absence of SDS, shows a double band suggesting an abnormal charge for the variant. Pt Metz exhibits an identity reaction with the control by double immunodiffusion. Upon activation by factor Xa, Pt Metz can generate amydolytic activity on Bz-Phe-Val-Arg-pNa (S2160), but only a very low clotting activity. Clear abnormalities are observed in the cleavage pattern of Pt Metz when monitored by SDS gel electrophoresis. The main feature are the accumulation of prethrombin l (Pl) and the appearance of abnormal intermediates migrating faster than Pl.


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