SITES OF "GLYCINE OXIDASE" ACTIVITY IN PROTEUS VULGARIS

1967 ◽  
Vol 13 (5) ◽  
pp. 551-556
Author(s):  
M. V. Nermut
Keyword(s):  
Plasma Membrane ◽  
Oxidase Activity ◽  
Proteus Vulgaris ◽  
Potassium Tellurite ◽  
Close Vicinity ◽  
Ultrathin Sections ◽  
Glycine Oxidase

The location of glycine oxidase activity in Proteus vulgaris was investigated using potassium tellurite and the technique of ultrathin sections. In 95% of cases, the tellurium deposits were found in the close vicinity of the plasma membrane, presumably at the inner side of it.

scholarly journals Penicillin-binding proteins and carboxypeptidase/transpeptidase activities in Proteus vulgaris P18 and its penicillin-induced stable L-forms

1982 ◽  
Vol 152 (3) ◽  
pp. 1042-1048
Author(s):  
A Rousset ◽  
M Nguyen-Distèche ◽  
R Minck ◽  
J M Ghuysen
Keyword(s):  
Plasma Membrane ◽  
Binding Proteins ◽  
Binding Protein ◽  
Penicillin Binding Protein ◽  
Proteus Vulgaris ◽  
Penicillin Binding Proteins

The originally penicillin-induced, wall-less stable L-forms of Proteus vulgaris P18, isolated by Tulasne in 1949 and since then cultured in he absence of penicillin, have kept the ability to synthesize the seven penicillin-binding proteins and the various DD- and LD-peptidase activities found in the parental bacteria and known to be involved in wall peptidoglycan metabolism. The stable L-forms, however, secrete during growth both the highly penicillin-sensitive, DD-carboxy-peptidase-transpeptidase penicillin-binding protein PBP4 (which in normal bacteria is relatively loosely bound to the plasma membrane) and the penicillin-insensitive LD-carboxypeptidase (which in normal bacteria is located in the periplasmic region).

scholarly journals Enhancing plasma membrane NADPH oxidase activity increases current output by diatoms in biophotovoltaic devices

2015 ◽  
Vol 12 ◽  
pp. 91-98 ◽  
Author(s):  
Anuphon Laohavisit ◽  
Alexander Anderson ◽  
Paolo Bombelli ◽  
Matthew Jacobs ◽  
Christopher J. Howe ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Nadph Oxidase ◽  
Oxidase Activity ◽  
Current Output ◽  
Nadph Oxidase Activity

scholarly journals Pre-apoptotic Alterations in Hepatocytes of TNF α-treated Galactosamine-sensitized Mice

1998 ◽  
Vol 46 (10) ◽  
pp. 1175-1183 ◽  
Author(s):  
Sabine Angermüller ◽  
Gerald Künstle ◽  
Gisa Tiegs
Keyword(s):  
Enzyme Activity ◽  
Plasma Membrane ◽  
Cytochrome Oxidase ◽  
Oxidase Activity ◽  
Chromatin Condensation ◽  
Dna Strand Breaks ◽  
Strand Breaks ◽  
High Enzyme ◽  
Dna Strand ◽  
High Enzyme Activity

Tumor necrosis factor (TNF) induces apoptotic death of hepatocytes in the galactosamine (GalN)-sensitized mouse liver after 5 hr. In our study, the most remarkable sign of the early stage of apoptosis was the focal rupture of the outer mitochondrial membrane. Parts of the inner membrane extended through the gap of the outer membrane, whereas the rest of the inner membrane still formed the cristae. This feature appeared in hepatocytes before chromatin condensation. With the diaminobenzidine technique for localization of cytochrome oxidase activity, the reaction product was detectable by light and electron microscopy. Ten percent of the hepatocytes were apoptotic, with condensed chromatin and high enzyme activity, 37% were pre-apoptotic, without chromatin condensation but high enzyme activity, and 53% had neither condensed chromatin nor a remarkable reaction product of cytochrome oxidase activity. Fas (APO-1, CD95) molecules on the plasma membrane of hepatocytes increased and were represented immunohistochemically in cells without chromatin condensation. DNA strand breaks were also detectable before chromatin aggregation. The results of this study indicate that mitochondria play a pivotal role in pre-apoptotic hepatocytes, together with an increase of the Fas molecule on the plasma membrane and with the occurrence of DNA strand breaks in the nucleus.

scholarly journals A CYTOCHEMICAL LOCALIZATION OF REDUCTIVE SITES IN A GRAM-POSITIVE BACTERIUM

1964 ◽  
Vol 20 (3) ◽  
pp. 361-375 ◽  
Author(s):  
Woutera van Iterson ◽  
W. Leene
Keyword(s):  
Plasma Membrane ◽  
Cell Periphery ◽  
Gram Positive ◽  
Cytochemical Localization ◽  
Potassium Tellurite ◽  
Thin Sections ◽  
Gram Positive Bacteria ◽  
Cytoplasmic Membranes ◽  
Reducing Activity ◽  
The One

In bacteria the exact location of a respiratory enzyme system comparable to that of the mitochondria of other cells has remained uncertain. On the one hand, the existence of particulate "bacterial mitochondria" has been advocated (Mudd); on the other hand, important enzymes of the respiratory chain were recovered in the cytoplasmic membranes associated with some granular material (Weibull). In order to gain insight into this question, sites of reducing activity were localized in thin sections of bacteria using the reduction of potassium tellurite as an indicator. When this salt was added to the culture medium of Bacillus subtilis, it turned out that in this Gram-positive organism the reduced product is strictly bound at two sites, and that the plasma membrane does not materially gain in electron opacity through deposition of the reduced product. The reduction product is found on or in the membranes of particular organelles, which may possibly be regarded as the mitochondrial equivalents in Gram-positive bacteria, and which are sometimes seen connected to the plasma membrane. The second location is in thin rod-like elements at the cell periphery, possibly the sites from which the flagella emerge.

Ultrastructure and sites of tetranitro-blue tetrazolium reduction of Lactobacillus casei

1968 ◽  
Vol 14 (8) ◽  
pp. 823-827 ◽  
Author(s):  
Joseph P. Brown ◽  
Mercedes R. Edwards ◽  
Paul J. VanDemark
Keyword(s):  
Plasma Membrane ◽  
Normal Control ◽  
Electron Micrographs ◽  
Lactobacillus Casei ◽  
Reduction Product ◽  
Lactobacillus Species ◽  
Blue Tetrazolium ◽  
Ultrathin Sections ◽  
Ultrastructural Characteristics ◽  
Tetrazolium Reduction

Cells of two strains of Lactobacillus casei incubated for 2–10 h in the presence of tetranitro-blue tetrazolium (TNBT) and mannitol were studied in electron micrographs of ultrathin sections. The reduction product tetranitro-blue diformazan (TNBF) was found to be predominantly associated with the plasma membrane and its derivatives. Untreated cells (normal control), as well as cells incubated with mannitol in absence of TNBT (dye control), or with omission of mannitol (substrate control) displayed ultrastructural characteristics, in general, similar to those previously reported for other Gram-positive bacilli, particularly Lactobacillus species.

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