scholarly journals Purification and properties of the alpha2beta2 complex of tryptophan synthetase of Proteus mirabilis.

1976 ◽  
Vol 251 (13) ◽  
pp. 3875-3880
Author(s):  
M Riverin ◽  
G R Drapeau
Keyword(s):  
Proteus Mirabilis ◽  
Purification And Properties ◽  
Tryptophan Synthetase

Purification and properties of the membrane-bound hydrogenase from Proteus mirabilis

1979 ◽  
Vol 567 (2) ◽  
pp. 511-521 ◽  
Author(s):  
Gerrit S. Shoenmaker ◽  
L.Fred Oltmann ◽  
Adrian H. Stouthamer
Keyword(s):  
Proteus Mirabilis ◽  
Purification And Properties ◽  
Membrane Bound

Purification and Properties of Glucosaminephosphate Isomerase of Proteus mirabilis

1982 ◽  
Vol 37 (5-6) ◽  
pp. 381-384 ◽  
Author(s):  
Blanca Cifuentes ◽  
C. Vicente
Keyword(s):  
Molecular Weight ◽  
Proteus Mirabilis ◽  
Temperature Optimum ◽  
Ph Optimum ◽  
Polyacrylamide Electrophoresis ◽  
Secondary Maximum ◽  
Purification And Properties

Abstract A glucosamine-P isomerase has been identified in Proteus mirabilis. The 113-fold purified enzyme exhibits a pH optimum of 7.5 with a secondary maximum at 8.5 and a temperature optimum at 37 °C. The apparent Km was 13.3 mᴍ for fructose-6-P and 18.8 mᴍ for ʟ-glutamine. Molecular weight of the enzyme has been estimated as 120000 and the protein can be dissociated in four subunits by SDS-polyacrylamide electrophoresis.

Purification and properties of the Proteus mirabilis catalase

1983 ◽  
Vol 61 (1) ◽  
pp. 8-14 ◽  
Author(s):  
Hélène M. Jouve ◽  
Sylvie Tessier ◽  
Jean Pelmont
Keyword(s):  
Molecular Weight ◽  
Proteus Mirabilis ◽  
Apparent Molecular Weight ◽  
Absorbance Spectrum ◽  
Physiological Conditions ◽  
Peroxidatic Activity ◽  
Purification And Properties ◽  
Main Fraction ◽  
Effects Of Ph ◽  
Isoelectric Ph

The purification of catalase from Proteus mirabilis has been described. The protein had four subunits of equal apparent molecular weight (MW 62 000). The enzyme was found to be slightly heterogenous after electrofocusing, the main fraction having an isoelectric pH of 4.8. No detectable peroxidatic activity was observed in physiological conditions. The absorbance spectrum and the effects of pH and temperature on catalase have also been described.

scholarly journals The purification and properties of the β-lactamase specified by the resistance factor R-1818 in Escherichia coli and Proteus mirabilis

1971 ◽  
Vol 123 (4) ◽  
pp. 493-500 ◽  
Author(s):  
J. W. Dale ◽  
J. T. Smith
Keyword(s):  
Escherichia Coli ◽  
Proteus Mirabilis ◽  
Gel Electrophoresis ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Resistance Factor ◽  
Ph Optimum ◽  
E Coli ◽  
R Factor ◽  
Purification And Properties

1. The β-lactamase specified by the R-1818 resistance factor in Escherichia coli was purified 300-fold; the resulting preparation gave a single peak on Sephadex G-100 and a single band on polyacrylamide-gel electrophoresis. 2. The β-lactamase specified by the same R-factor in Proteus mirabilis was purified over 2000-fold, but was still far from pure. The specific activity of this preparation was one-fifth that of the purified enzyme from E. coli. 3. The two enzymes were shown to be identical as regards substrate specificity, pH optimum, Km values and molecular weight. 4. It is suggested that the low β-lactamase activity of extracts of P. mirabilis (R-1818), about 5% of that from E. coli (R-1818) in crude extracts, could be due to inefficient transcription of the R-factor DNA by Proteus RNA polymerase.

Ultrastructure of periplasmic bodies in gram-negative bacteria

1990 ◽  
Vol 48 (3) ◽  
pp. 640-641
Author(s):  
Xie Nianming ◽  
Ding Shaoqing ◽  
Wang Luping ◽  
Yuan Zenglin ◽  
Zhan Guolai ◽  
...  
Keyword(s):  
Electron Microscope ◽  
Campylobacter Jejuni ◽  
Proteus Mirabilis ◽  
Shigella Flexneri ◽  
Morphological Description ◽  
Gram Negative Bacteria ◽  
Periplasmic Space ◽  
Clostridium Tetani ◽  
Gram Negative ◽  
Brucella Canis

Perhaps the data about periplasmic enzymes are obtained through biochemical methods but lack of morphological description. We have proved the existence of periplasmic bodies by electron microscope and described their ultrastructures. We hope this report may draw the attention of biochemists and mrophologists to collaborate on researches in periplasmic enzymes or periplasmic bodies with each other.One or more independent bodies may be seen in the periplasmic space between outer and inner membranes of Gram-negative bacteria, which we called periplasmic bodies. The periplasmic bodies have been found in seven species of bacteria at least, including the Pseudomonas aeroginosa. Shigella flexneri, Echerichia coli. Yersinia pestis, Campylobacter jejuni, Proteus mirabilis, Clostridium tetani. Vibrio cholerae and Brucella canis.

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