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.

scholarly journals On the Glycogen in Escherichia coli B; Variations in Molecular Weight during Growth. I.

1957 ◽  
Vol 11 ◽  
pp. 757-762 ◽  
Author(s):  
T. Holme ◽  
T. Laurent ◽  
H. Palmstierna ◽  
Arne Magnéli ◽  
Arne Magnéli ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Molecular Weight ◽  
Escherichia Coli B

scholarly journals Separation, purification and properties of β-lactamase I and β-lactamase II from Bacillus cereus 569/H/9

1974 ◽  
Vol 143 (1) ◽  
pp. 115-127 ◽  
Author(s):  
Richard B. Davies ◽  
E. P. Abraham ◽  
J. Melling
Keyword(s):  
Molecular Weight ◽  
Bacillus Cereus ◽  
Large Scale ◽  
Cysteine Residue ◽  
Peptide Fragment ◽  
Tryptic Digest ◽  
Purification And Properties ◽  
Carbohydrate Complex ◽  
Entire Sequence ◽  
Main Components

1. A procedure was devised which is suitable for the isolation of β-lactamase I and β-lactamase II from Bacillus cereus 569/H/9 on a large scale. After adsorption on to Celite both enzymes were eluted in good yield and separated by chromatography on Sephadex CM-50. 2. β-Lactamase I was separated into three main components by isoelectric focusing and into two components by chromatography. 3. The Zn2+-requiring β-lactamase II obtained by this procedure had a lower molecular weight (22000) than β-lactamase I (28000) and also differed from the latter in containing one cysteine residue. 4. The β-lactamase II contained no carbohydrate, but showed the thermostability of the enzyme isolated earlier as a protein–carbohydrate complex. 5. Amino acid analyses and tryptic-digest ‘maps’ indicate that some degree of homology between β-lactamase I and β-lactamase II is possible, but that β-lactamase I is not composed of the entire sequence of β-lactamase II together with an additional peptide fragment. 6. A 6-methylpenicillin and a 7-methylcephalosporin showed much lower affinities for both enzymes than did penicillins and cephalosporins themselves.

Propriétés physiques et chimiques des tryptophanases de cinq espèces d'Entérobactériaceae

1975 ◽  
Vol 21 (6) ◽  
pp. 828-833 ◽  
Author(s):  
C. Simard ◽  
A. Mardini ◽  
L. M. Bordeleau
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Molecular Weight ◽  
Sedimentation Coefficient ◽  
Species Differentiation ◽  
Proteus Vulgaris ◽  
Amino Acids Composition ◽  
Propriétés Physiques ◽  
Tryptophan Content ◽  
Escherichia Coli B

The molecular weight, sedimentation coefficient, and amino acids composition were determined on five tryptophanases (TPases) from Escherichia coli B and E. aurescens, Shigella alkalescens, and Proteus vulgaris and P. morganii. These TPases have identical sedimentation profile and coefficient (9.6 S), and the same molecular weight (220 000). Each enzyme is constituted of four identical subunits having a molecular weight of 55 000. The amino acids composition of these TPases is very similar, with the exception of P. morganii and P. vulgaris TPases which present significative variations in basic amino acids and tryptophan content. The species differentiation of the coli group cannot be made on their TPase characteristics only, contrary to P. morganii and P. vulgaris which can be differentiated between them and from the coli group. [Journal translation]

scholarly journals On the Glycogen in Escherichia coli B; Variations in Molecular Weight during Growth. II.

1958 ◽  
Vol 12 ◽  
pp. 1559-1563 ◽  
Author(s):  
T. Holme ◽  
T. Laurent ◽  
H. Palmstierna ◽  
T. Linderot ◽  
S. Veige ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Molecular Weight ◽  
Escherichia Coli B

scholarly journals On the Glycogen in Escherichia coli B; Variations in Molecular Weight during Growth. III.

1958 ◽  
Vol 12 ◽  
pp. 1564-1567 ◽  
Author(s):  
T. Holme ◽  
Lembitu Reio ◽  
Ole Tvedten ◽  
T. Linderot ◽  
S. Veige ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Molecular Weight ◽  
Escherichia Coli B

scholarly journals Primary structure of major outer-membrane protein I (ompF protein, porin) of Escherichia coli B/r

1982 ◽  
Vol 203 (1) ◽  
pp. 33-43 ◽  
Author(s):  
R Chen ◽  
C Krämer ◽  
W Schmidmayr ◽  
U Chen-Schmeisser ◽  
U Henning
Keyword(s):  
Escherichia Coli ◽  
Molecular Weight ◽  
Outer Membrane ◽  
Primary Structure ◽  
Transmembrane Proteins ◽  
Low Molecular Weight ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Preliminary Communication ◽  
Escherichia Coli B

In the outer membrane of Gram-negative bacteria hydrophilic pores exist, allowing the diffusion of various low-molecular-weight solutes. These pores are formed by proteins, the porins. In a preliminary communication [Chen, Krämer, Schmidmayr & Henning (1979) Proc. Natl. Acad. Sci. U.S.A. 76, 5014-5017] we presented the primary structure of one of these porins, the 340-amino-acid-residue protein I (ompF protein) from Escherichia coli B/r. In the present paper we give the experimental evidence for this sequence. Two tryptophan positions, one valine position, two aspartic acid positions and nine out of 82 amide determinations have been corrected. To aid further studies on this class of transmembrane proteins, the isolation of most of the constituent peptides is documented.

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