Biomedical subjects
Publications and source records attributed to L Alföldi.
Hfr x F- recombinational genome interactions are simulated by a computer program. Genotype spectrums of selected samples from Hfr x F- crosses of Escherichia coli, found in the published literature, are reproduced. Relevance of the findings for interpretation of conjugational results in Escherichia coli is discussed.
A procedure is presented in which model populations, simulating progenies obtained from Escherichia coli Hfr x F- crosses, are generated. The procedure seems to be appropriate for visualizing hidden features of the genetic analysis, which are not detected by the conjugational crosses.
Model populations, simulating progenies obtained from Escherichia coli Hfr x F- crosses, are generated. Linkage relations and exchange frequencies are expressed in these populations in complex, in some cases, even paradoxical manner. It is demonstrated that the origin of the complexities is located in the particular allelic configuration of the genotypes, characteristic for all exconjugant and selected populations.
This essay describes the author's studies with bacteria in post-war Hungary; the difficulties encountered, with funding, collaboration and publication; and how the Szeged Institute consolidated itself as the one outstanding scientific institute in Eastern Europe, with the author at the helm.
Authors describe a case of isolated posttraumatic neuropraxy of the musculocutaneous nerve. With the presentation of this very rare case attention is called, based on literary date, to the fact that the above injury can be mixed with the distal tendon rupture of the biceps.
Polyethylene glycol-(PEG)-induced fusion of both procaryotic and eucaryotic microorganisms seems to be a good technique for constructing hybrid microorganisms. Though the data published show that the fusion technique can be successfully applied for genetic analysis even in systems having no natural way to do it, further studies are needed to find, for each system, the conditions where it works in predictable ways.
Ability to produce megacin A, a bacteriocin of B. megaterium, was transferred from the strain B. megaterium 216 into auxotrophic derivatives of the strain B. megaterium KM via protoplast fusion and polyethylene-glycol-induced protoplast transformation by plasmid DNA, respectively. A 30.9 megadalton plasmid was detected in cells with MegA phenotype, and the loss of this phenotype was accompanied in each case with the elimination of that plasmid. The megacinogenic plasmid pBM309 has a single site for both BamHI and XhoI. It is cleaved by the endonucleases SalI, BglII, PstI, PvuII, and EcoRI into 3, 3, 4, 4, and 9 fragments, respectively. The physical map of this plasmid is presented.
Direct selection for recombinants by supplemented minimal media from polyethylene-glycol (PEG)-induced fusion of protoplasts of polyauxotrophic strains of B. megaterium revealed striking physiological influences on the yield of recombinants. Cytoplasmic state of the protoplasts to be fused, rather than genetic events, determined the number of colonies obtained on the selection media. It is suggested that the physiological effects primarily influenced the ability of the fused protoplasts to revert to bacillary form.
Protoplasts of Bacillus megaterium, incubated at 50 degrees C for 120 min, lost the ability to revert to bacillary form. Such heat-inactivated protoplasts, however, produced recombinants when fused by polyethylene glycol treatment with normal protoplasts. Although this differential inactivation effect is not yet fully reproducible, reciprocal inactivations of the parental protoplasts in genetic crosses have clearly shown that for protoplast fusion (i) either of the parents may serve as the viable recipient for markers coming from the heated parental protoplasts, and (ii) either of the parents may be rendered nonviable and yet, when fused with a viable partner, contribute to formation of a recombinant. Heat inactivation seems to provide a way to counterselect when few markers are available and one of the parents is prototrophic.
Protoplasts of two doubly auxotrophis strains of Bacillus megaterium were fused by nascent calcium phosphate or by polyethylene glycol treatment, and then allowed to revert to bacillary form on selection media. The colonies formed were analyzed and found to be mixed populations of individual bacteria apparently containing parental, recombinant, and segregating genotypes. The evidence suggested that segregation was transitory, lasting only for a few clonings and reisolations.
Protoplasts of Bacillus megaterium readily reverted to bacillary form in liquid media and when plated in a soft-agar layer onto the surface of appropriate agar media. Three phases of the reversion sequence could be differentiated by phase contrast microscopy: (i) increase in size of the individual protoplasts, (ii) non oriented division of the protoplasts and (iii) outgrowth of the bacillary forms. With time-lapse photomicrography, reversion sequences of single protoplasts were demonstrated.
Photomicrographic evidence of reversion of Bacillus megaterium protoplasts to the bacillary form on soft agar plates hypertonic medium is demonstrated.
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(a) The measured L-serine deaminating activity of a crude bacterial extract may originate from L-serine deaminase, from biosynthetic L-threonine deaminase, or from degradative L-serine deaminase. Nevertheless, the contribution of the individual enzymes can be determined.(b) About a half of the L-serine deaminating activity of wild type E. coli bacteria, grown in synthetic minimal medium, originates from L-serine deaminase and about half from biosynthetic L-threonine deaminase.(c) Ninety percent of L-serine deaminating activity of wild type E. coli bacteria, grown in yeast extract-tryptone medium, originates from L-serine deaminase, and the remainging ten percent from the degradative L-threonine deaminase.(d) Conditions have been established in which threonine deaminases are eliminated and the activity of L-serine deaminase alone could be measured, even in crude extracts.
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The native l-serine deaminase (l-serine hydrolyase, deaminating, EC 4.2.1.13) of Escherichia coli K-12, which seems to be a very labile protein, is rather stable in concentrated solution. Dilution rapidly inactivates it, but in the presence of a saturating concentration of l-serine the molecule is protected from inactivation. It is a very specific enzyme; l-serine is the sole substrate with a K(m) value of 6.60 x 10(-3)m. d-Serine and l-cysteine are competitive inhibitors. Substrate saturation curves of the native enzyme show sigmoid shape, whereas the enzyme liberated from the bacteria in the presence of l-serine exhibits normal Michaelis-Menten kinetics.
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