scholarly journals A PHASE CONTRAST STUDY OF THE CHROMATINIC BODIES OF ESCHERICHIA COLI SUBSEQUENT TO ULTRAVIOLET IRRADIATION

1956 ◽  
Vol 71 (4) ◽  
pp. 462-473 ◽  
Author(s):  
J. R. Cortelyou ◽  
L. M. Amundson ◽  
M. A. McWhinnie
1978 ◽  
Vol 76 (3) ◽  
pp. 587 ◽  
Author(s):  
Drago Petranović ◽  
Mirjana Petranović ◽  
Ranka Nožinić ◽  
Željko Trgovčević ◽  
Drago Petranovic ◽  
...  

2001 ◽  
Vol 183 (17) ◽  
pp. 5041-5049 ◽  
Author(s):  
Steven B. Zimmerman ◽  
Lizabeth D. Murphy

ABSTRACT The genomic DNA of bacteria is contained in one or a few compact bodies known as nucleoids. We describe a simple procedure that retains the general shape and compaction of nucleoids from Escherichia coli upon cell lysis and nucleoid release from the cell envelope. The procedure is a modification of that used for the preparation of spermidine nucleoids (nucleoids released in the presence of spermidine) (T. Kornberg, A. Lockwood, and A. Worcel, Proc. Natl. Acad. Sci. USA 71:3189–3193, 1974). Polylysine is added to prevent the normal decompaction of nucleoids which occurs upon cell lysis. Nucleoids retained their characteristic shapes in lysates of exponential-phase cells or in lysates of cells treated with chloramphenicol or nalidixate to alter nucleoid morphology. The notably unstable nucleoids of rifampin-treated cells were obtained in compact, stable form in such lysates. Nucleoids released in the presence of polylysine were easily processed and provided well-defined DNA fluorescence and phase-contrast images. Uniform populations of nucleoids retaining characteristic shapes could be isolated after formaldehyde fixation and heating with sodium dodecyl sulfate.


1980 ◽  
Vol 83 (2) ◽  
pp. 323
Author(s):  
Erika Salaj-Šmic ◽  
Drago Petranović ◽  
Mirjana Petranović ◽  
Željko Trgovčević ◽  
Erika Salaj-Smic ◽  
...  

1964 ◽  
Vol 21 (3) ◽  
pp. 385-396 ◽  
Author(s):  
D. Gilmour ◽  
P. M. Robinson

The A substance of glycerol-treated myofibrils of the femoral muscles of the locust Gastrimargus musicus (Fabr.), removed by a salt solution of high ionic strength, has the properties of actomyosin. A phase contrast study of these fibrils, contracted by the addition of ATP, has revealed that the A bands of most myofibrils shorten during contraction. Changes in density within the A band lead to the formation of Cm and Cz bands while I bands are still present. The A band region between the contraction bands is of much lower density than it is in the uncontracted fibril. During contraction in some fibrils the I bands disappeared and the A bands remained unchanged in length until contraction bands appeared. These results have been interpreted in terms of coiling and stretching of the thick filaments of the sarcomere.


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