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]

Mechanism of action of an inhibitor from Proteus vulgaris on cell-free protein synthesis by Escherichia coli B

1969 ◽  
Vol 15 (2) ◽  
pp. 159-164
Author(s):  
J. J. McEvoy ◽  
W. E. Inniss
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Protein Synthesis ◽  
Mechanism Of Action ◽  
Ribonucleic Acid ◽  
Proteus Vulgaris ◽  
Flash Evaporation ◽  
Free System ◽  
Messenger Ribonucleic Acid ◽  
Escherichia Coli B

An inhibitory substance(s) has been found in S-30 fractions from Proteus vulgaris which prevented an Escherichia coli B cell-free system from incorporating a mixture of 14C-amino acids, L-phenylalanine-14C, or L-lysine-14C into protein, as directed by natural messenger ribonucleic acid, polyuridylic acid, or polyadenylic acid respectively. Similar results were obtained when the inhibitor was isolated from S-100 fractions by using dialysis, concentration of the dialysate by flash evaporation, hydrolysis, evaporation to dryness, dissolution to the original volume in distilled water, and neutralization. The effect of the inhibitor on the various individual reactions involved in protein synthesis was examined. No effect was found on the activation of amino acids as determined by the formation of L-phenylalanine-14C hydroxamate isolated chromatographically or by adenosine triphosphate – pyrophosphate exchange. Also no inhibition of L-phenylalanine-14C attachment to transfer ribonucleic acid occurred. However, ribosome-dependent reactions were markedly inhibited. The mechanism of action of the inhibitor appeared to be the prevention of binding of phenylalanyl-transfer ribonucleic acid to the ribosomes.

Distinction des tryptophanases de cinq espèces d'Entérobactériaceae par les groupements sulfhydryles

1975 ◽  
Vol 21 (6) ◽  
pp. 841-845 ◽  
Author(s):  
C. Simard ◽  
A. Mardini ◽  
L. M. Bordeleau
Keyword(s):  
Escherichia Coli ◽  
Molecular Weight ◽  
Quaternary Structure ◽  
Sulfhydryl Groups ◽  
Enzyme Structure ◽  
Proteus Vulgaris ◽  
Sh Groups ◽  
Enzyme Substrate ◽  
Escherichia Coli B

We have studied the sulfhydryl groups (—SH) on the tryptophanases (TPases) from Escherichia coli B. and E. aurescens, Shigella alkalescens, and Proteus vulgaris and P. morganii. The coli group and the P. morganii apo TPases have 20 —SH groups per mole of enzyme, whereas P. vulgaris apo TPase has 16. In coli group TPases, there are 16 —SH groups on the mole surface and they are all implicated in the activity and the enzyme–substrate bond. Proteus morganii TPase has 8 surface —SH groups, 4 of which are implicated in the activity; the remaining 12 —S H groups are located inside the mole and take part in the activity and the enzyme—substrate bond. Proteus vulgaris TPase has 4 surface —SH groups which are constitutive of the enzyme structure, whereas the 12 remaining —SH groups are located inside the mole and take part in the activity and the enzyme–substrate bond. It is concluded that Proteus TPases are molecules which have inverted quaternary structure in comparison to those of the coli group. The studied TPases have four subunits, each of them is constituted of one polypeptidic chain having a molecular weight of 55 000. [Journal translation]

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 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

Isolation, purification, and partial characterization of type V-A hemagglutinin from Escherichia coli GV-12, O1:H-

1982 ◽  
Vol 152 (2) ◽  
pp. 757-761
Author(s):  
V L Sheladia ◽  
J P Chambers ◽  
J Guevara ◽  
D J Evans
Keyword(s):  
Escherichia Coli ◽  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Sedimentation Coefficient ◽  
Amino Terminus ◽  
N Terminus ◽  
Type V

A hemagglutinin which specifically agglutinates human type A erythrocytes (mannose resistant) was isolated from the growth medium of cultures of Escherichia coli GV-12, serotype O1:H-, and purified by chromatography on Bio-Gel A-1.5 and DEAE-Sephadex A-25. The purity of the hemagglutinin was established by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoelectrophoresis. N-terminus analysis indicated that only asparagine resides on the amino terminus. The native hemagglutinin is an aggregate exhibiting a sedimentation coefficient of 9.25, which corresponds to a molecular weight of approximately 200,000. The monomeric molecular weight was found to be approximately 16,300. Amino acid analysis indicated that the hemagglutinin consists of 131 residues, corresponding to a molecular weight of 13,400.

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.

THE EFFECT OF 3000–4000 Å LIGHT ON THE SYNTHESIS OF β-GALACTOSIDASE AND BACTERIOPHAGES BY ESCHERICHIA COLI B

1967 ◽  
Vol 13 (1) ◽  
pp. 69-79 ◽  
Author(s):  
S. J. Webb ◽  
J. Singh Bhorjee
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Dna Replication ◽  
Glutamic Acid ◽  
Strong Correlation ◽  
Sublethal Doses ◽  
Time Periods ◽  
Escherichia Coli B

The irradiation of Escherichia coli B with sublethal doses of 3000–4000 Å light prevented the microorganisms from manufacturing β-galactosidase and T2 and T7 coliphages. Inhibition occurred only if the cells were irradiated immediately after their contact with the inducer lactose or infection with T2 and T7 phages. If, before irradiation the cells were allowed to incubate for 15 min after the addition of lactose or the coliphages to the cells, little effect of the light was found. The uptake of uracil and amino acids by washed cells was more rapid in the first 15 min than during later time periods while thymine uptake did not begin until the first 15 min had elapsed. The 3000–4000 Å light inhibited the uptake of arginine and thymine but not uracil or glutamic acid. The addition of 5% inositol inhibited the synthesis of β-galactosidase and the uptake of14C-labelled metabolites. Since there was a strong correlation between the degree to which arginine and thymine uptakes were inhibited by the light or inositol, it appears that the production of a protein during the first 15 min is intimately connected with DNA replication and the synthesis of induced enzymes.

Sign in / Sign up

Export Citation Format

Share Document