scholarly journals Identification and Characterization of Large Plasmids in Rhizobium meliloti using Agarose Gel Electrophoresis

1979 ◽  
Vol 113 (2) ◽  
pp. 229-242 ◽  
Author(s):  
F. CASSE ◽  
C. BOUCHER ◽  
J. S. JULLIOT ◽  
M. MICHEL ◽  
J. DENARIE
2008 ◽  
Vol 129 (3) ◽  
pp. 451-458 ◽  
Author(s):  
Christopher R. McCudden ◽  
Stephanie P. Mathews ◽  
Shirley A. Hainsworth ◽  
John F. Chapman ◽  
Catherine A. Hammett-Stabler ◽  
...  

Genomics ◽  
1989 ◽  
Vol 5 (4) ◽  
pp. 915-924 ◽  
Author(s):  
S.J. Odelberg ◽  
R. Plaetke ◽  
J.R. Eldridge ◽  
L. Ballard ◽  
P. O'Connell ◽  
...  

1984 ◽  
Vol 5 (4) ◽  
pp. 202-208 ◽  
Author(s):  
Philip Serwer ◽  
Elena T. Moreno ◽  
Shirley J. Hayes ◽  
Philip Berger ◽  
Marie Langham ◽  
...  

1996 ◽  
Vol 76 (03) ◽  
pp. 453-459 ◽  
Author(s):  
Virginie Siguret ◽  
Anne-Sophie Ribba ◽  
Olivier Christophe ◽  
Ghislaine Chérel ◽  
Bernadette Obert ◽  
...  

SummaryThe interacting domain of vWF with platelet GPIb has been shown to overlap the large A1 loop formed by the intra-chain disulfide bond linking Cys 509 to Cys 695. In order to further investigate the role of the conformation of this region, we have expressed in COS-7 cells three mutated full-length recombinant vWFs (rvWFs) in which the substitutions Cys509Gly, Cys509Arg or Cys695Gly have been introduced by site-directed mutagenesis. SDS-agarose gel electrophoresis demonstrated an impaired multimerization of the mutants with undetectable high molecular weight multimers and a decrease of the relative amounts of the intermediate sized multimers. Binding analysis showed that rvWFC509G and rvWFC509R did not interact with botrocetin but spontaneously interacted with GPIb; the latter binding remained unchanged in the presence of ristocetin. This indicates that the substitution of Cys509 by Gly or Arg creates a conformation of vWF that increases its binding to GPIb. In contrast, rvWFC695G which did not react with botrocetin was also unable to interact with GPIb even in the presence of ristocetin, indicating that sequences interacting with GPIb are masked and/or disrupted. In conclusion, the substitution of each of the Cys509 and 695 results in mutant proteins which may be “locked” into active or inactive conformations in regard to the binding to platelet GPIb receptor.


1985 ◽  
Vol 147 (2) ◽  
pp. 353-363 ◽  
Author(s):  
Melvin H. Gottlieb ◽  
Clifford J. Steer ◽  
Alasdair C. Steven ◽  
Andreas Chrambach

1979 ◽  
Vol 113 (1) ◽  
pp. 73-81 ◽  
Author(s):  
A. F. Jamieson ◽  
D. A. Bremner ◽  
P. L. Bergquist ◽  
H. E. D. Lane

1981 ◽  
Vol 27 (3) ◽  
pp. 271-278 ◽  
Author(s):  
Wesley E. Kloos ◽  
Barbara S. Orban ◽  
Diane D. Walker

A total of 342 staphylococci representing 13 different recognized species were screened for plasmid composition using agarose gel electrophoresis techniques. Plasmids of molecular weight (MW) 30 × 106 or larger in size were uncommon in staphylococci. Moderately large plasmids of MW 15 × 106 to 29 × 106 were not or only occasionally found in the species Staphylococcus sciuri, S. intermedius, S. hyicus, or S. simulans, but were common in S. aureus (55%) and members of the S. epidermidis (79%) and S. saprophyticus (86%) species groups. Small plasmids were common in most of the species. They produced more complex profiles in simian subspecies or biotypes than in human subspecies or biotypes, e.g., in the species S. warneri, S. haemolyticus, S. cohnii, S. xylosus, and S. aureus. Although some of the species appeared to have rather unique plasmid patterns, we would currently hesitate to use this feature as a taxonomic character, considering the occurrence of exceptional strains and possible plasmid transfer between species.


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