Primary sequence of tRNA1Valfrom Escherichia coli. B. I. Oligonucleotide sequences of digests of Escherichia coli tRNA1valwith RNase T1and pancreatic RNase

Biochemistry ◽  
1971 ◽  
Vol 10 (17) ◽  
pp. 3269-3277 ◽  
Author(s):  
Susumu Nishimura ◽  
Fumio Harada ◽  
Fumiko Kimura
Keyword(s):  
Escherichia Coli ◽  
Primary Sequence ◽  
Pancreatic Rnase ◽  
Escherichia Coli B

A ribosomal-bound aminopeptidase in Escherichia coli B: purification and properties

1970 ◽  
Vol 48 (11) ◽  
pp. 1181-1188 ◽  
Author(s):  
A. J. Dick ◽  
A. T. Matheson ◽  
J. H. Wang
Keyword(s):  
Escherichia Coli ◽  
Molecular Weight ◽  
Large Scale ◽  
The Other ◽  
Stable Form ◽  
Peptidase Activity ◽  
Purification And Properties ◽  
Pancreatic Rnase ◽  
High Concentrations ◽  
Escherichia Coli B

Two procedures have been developed for the large-scale purification from Escherichia coli B of a ribosomal-bound aminopeptidase in a stable form: one involving the digestion of the ribosome with pancreatic RNase and the other the selective removal of the aminopeptidase from the ribosomal surface with NH4Cl. The enzyme, as isolated from the ribosome, is a polymeric protein composed of monomeric units with a molecular weight of approximately 60 000 Daltons. The purified enzyme is activated by β-mercaptoethanol or dithiothreitol, although at high concentrations dithiothreitol inhibits peptidase activity. Propylene glycol also inhibits the enzyme. The enzyme is stable at 70° in the presence of free SH groups.

Sites of Adsorption of the Bacteriophages T3 and T5 on the Wall of Escherichia Coli B.

1967 ◽  
Vol 25 ◽  
pp. 96-97
Author(s):  
Manfred E. Bayer
Keyword(s):  
Escherichia Coli ◽  
Cell Wall ◽  
Electron Microscope ◽  
Uranyl Acetate ◽  
E Coli ◽  
Receptor Sites ◽  
Rigid Cell Wall ◽  
Host Cell Surface ◽  
Bacterial Viruses ◽  
Escherichia Coli B

Bacterial viruses adsorb specifically to receptors on the host cell surface. Although the chemical composition of some of the cell wall receptors for bacteriophages of the T-series has been described and the number of receptor sites has been estimated to be 150 to 300 per E. coli cell, the localization of the sites on the bacterial wall has been unknown.When logarithmically growing cells of E. coli are transferred into a medium containing 20% sucrose, the cells plasmolize: the protoplast shrinks and becomes separated from the somewhat rigid cell wall. When these cells are fixed in 8% Formaldehyde, post-fixed in OsO4/uranyl acetate, embedded in Vestopal W, then cut in an ultramicrotome and observed with the electron microscope, the separation of protoplast and wall becomes clearly visible, (Fig. 1, 2). At a number of locations however, the protoplasmic membrane adheres to the wall even under the considerable pull of the shrinking protoplast. Thus numerous connecting bridges are maintained between protoplast and cell wall. Estimations of the total number of such wall/membrane associations yield a number of about 300 per cell.

scholarly journals Separation and Characterization of Deoxyribonucleases of Escherichia coli B

1966 ◽  
Vol 241 (13) ◽  
pp. 3090-3096
Author(s):  
Sally E. Jorgensen ◽  
James F. Koerner
Keyword(s):  
Escherichia Coli ◽  
Escherichia Coli B

scholarly journals Crystalline l-Asparaginase from Escherichia coli B

1970 ◽  
Vol 245 (14) ◽  
pp. 3708-3715 ◽  
Author(s):  
Peter P.K. Ho ◽  
Elizabeth B. Milikin ◽  
Jesse L. Bobbitt ◽  
Edward L. Grinnan ◽  
Philip J. Burck ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Escherichia Coli B
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