scholarly journals Recircularization and Autonomous Replication of a Sheared R-Factor DNA Segment in Escherichia coli Transformants

1973 ◽  
Vol 70 (5) ◽  
pp. 1293-1297 ◽  
Author(s):  
S. N. Cohen ◽  
A. C. Y. Chang
1971 ◽  
Vol 18 (3) ◽  
pp. 287-297 ◽  
Author(s):  
T. J. Foster ◽  
T. G. B. Howe

SUMMARYRecombination between chloramphenicol-sensitive (Cms) mutants of Rl, and R100, has been demonstrated inEscherichia coliK12rec+; it occurs at reduced frequency inrecBandrecC, and is not detectable inreeA, indicating that R factor recombination depends on host functions. Some mutants of R1 also recombine with an R100 mutant in a similar way.recAcells carrying an R1 and an R100 Cmsmutant (hetero-R state) have a low level of chloramphenicol-resistance, and form a chloramphenicol acetyl transferase that has lower specific activity than enzyme from hosts carrying wild-type or recombinant factors. These results suggest the occurrence of interallelic complementation between mutant R factors.


1971 ◽  
Vol 123 (4) ◽  
pp. 501-505 ◽  
Author(s):  
J. W. Dale

1. The amino acid composition of the β-lactamase from E. coli (R-1818) was determined. 2. The R-1818 β-lactamase is inhibited by formaldehyde, hydroxylamine, sodium azide, iodoacetamide, iodine and sodium chloride. 3. The Km values for benzylpenicillin, ampicillin and oxacillin have been determined by using the R-factor enzyme from different host species. The same values were obtained, irrespective of the host bacterium. 4. The molecular weight of the enzyme was found to be 44600, and was the same for all host species. 5. The relationship of R-1818 and R-GN238 β-lactamases is discussed.


Plasmid ◽  
1981 ◽  
Vol 6 (1) ◽  
pp. 78-85
Author(s):  
Anna Fietta ◽  
Guido Grandi ◽  
Massimo Malcovati ◽  
Gianna Valentini ◽  
Vittorio Sgaramella ◽  
...  
Keyword(s):  
R Factor ◽  

1972 ◽  
Vol 25 (8) ◽  
pp. 483-484 ◽  
Author(s):  
SHINICHI KONDO ◽  
HARUO YAMAMOTO ◽  
HIROSHI NAGANAWA ◽  
HAMAO UMEZAWA ◽  
SUSUMU MITSUHASHI

1972 ◽  
Vol 130 (1) ◽  
pp. 55-62 ◽  
Author(s):  
J. Melling ◽  
G. K. Scott

Purified penicillinase, in gram quantities, has been prepared from Escherichia coli strain W3310 by using methods developed to handle large amounts of material. The final product had a specific enzyme activity of 3.08 units/μg of protein, which was over twice as high as that reported previously (Datta & Richmond, 1966). The purified enzyme was similar to that from E. coli strain TEM, but different in molecular weight and some other respects. The differences observed may be a result of the greater purity obtained.


1976 ◽  
Vol 93 (1) ◽  
pp. 103-110 ◽  
Author(s):  
D. J. Tweats ◽  
M. J. Thompson ◽  
R. J. Pinney ◽  
J. T. Smith

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