scholarly journals Optimal Conditions and Substrate Specificity for Trehalose Production by Resting Cells of Arthrobacter crystallopoietes N-08

2011 ◽  
Vol 16 (4) ◽  
pp. 357-363 ◽  
Author(s):  
Yi-Seul Seo ◽  
Kwang-Soon Shin
Keyword(s):  
Substrate Specificity ◽  
Resting Cells ◽  
Optimal Conditions ◽  
Arthrobacter Crystallopoietes

scholarly journals Haloalkane Dehalogenase LinB Is Responsible for β- and δ-Hexachlorocyclohexane Transformation in Sphingobium indicum B90A

2006 ◽  
Vol 72 (9) ◽  
pp. 5720-5727 ◽  
Author(s):  
Poonam Sharma ◽  
Vishakha Raina ◽  
Rekha Kumari ◽  
Shweta Malhotra ◽  
Charu Dogra ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Substrate Specificity ◽  
Incubation Mixture ◽  
Resting Cells ◽  
Haloalkane Dehalogenase ◽  
Hch Isomers ◽  
Hexachlorocyclohexane Isomers

ABSTRACT Incubation of resting cells of Sphingobium indicum B90A, Sphingobium japonicum UT26, and Sphingobium francense Sp+ showed that they were able to transform β- and δ-hexachlorocyclohexane (β- and δ-HCH, respectively), the most recalcitrant hexachlorocyclohexane isomers, to pentachlorocyclohexanols, but only resting cells of strain B90A could further transform the pentachlorocyclohexanol intermediates to the corresponding tetrachlorocyclohexanediols. Moreover, experiments with resting cells of Escherichia coli expressing the LinB proteins of strains B90A, UT26, and Sp+ indicated that LinB was responsible for these transformations. Purified LinB proteins from all three strains also effected the formation of the respective pentachlorocyclohexanols. Although the three LinB enzymes differ only marginally with respect to amino acid sequence, they showed interesting differences with respect to substrate specificity. When LinB from strain B90A was incubated with β- and δ-HCH, the pentachlorocyclohexanol products were further transformed and eventually disappeared from the incubation mixtures. In contrast, the LinB proteins from strains UT26 and Sp+ could not catalyze transformation of the pentachlorocyclohexanols, and these products accumulated in the incubation mixture. A mutant of strain Sp+ lacking linA and linB did not degrade any of the HCH isomers, including β-HCH, and complementation of this mutant by linB from strain B90A restored the ability to degrade β- and δ-HCH.

scholarly journals Optimal conditions for cultivation of Rhodococcus sp. N-774 and for conversion of acrylonitrile to acrylamide by resting cells.

1987 ◽  
Vol 51 (12) ◽  
pp. 3201-3206 ◽  
Author(s):  
Ichiro WATANABE ◽  
Yoshiaki SATOH ◽  
Kanehiko ENOMOTO ◽  
Susumu SEKI ◽  
Keiichi SAKASHITA
Keyword(s):  
Resting Cells ◽  
Optimal Conditions ◽  
Rhodococcus Sp

scholarly journals Optimal Conditions for Cultivation ofRhodococcussp. N-774 and for Conversion of Acrylonitrile to Acrylamide by Resting Cells

1987 ◽  
Vol 51 (12) ◽  
pp. 3201-3206
Author(s):  
Ichiro Watanabe ◽  
Yoshiaki Satoh ◽  
Kanehiko Enomoto ◽  
Susumu Seki ◽  
Keiichi Sakashita
Keyword(s):  
Resting Cells ◽  
Optimal Conditions

Ultrastructure of Melosira resting cell rejuvenation

1984 ◽  
Vol 42 ◽  
pp. 734-735
Author(s):  
C. E. M. Bourne ◽  
L. Sicko-Goad
Keyword(s):  
Electron Microscopy ◽  
Lake Michigan ◽  
Light And Electron Microscopy ◽  
Resting Cells ◽  
Planktonic Diatoms ◽  
Resting Cell ◽  
Vegetative Survival ◽  
Cytological Changes ◽  
Recent Attention ◽  
Freshwater Diatom

Much recent attention has been focused on vegetative survival forms of planktonic diatoms and other algae. There are several reports of extended vegetative survival of the freshwater diatom Melosira in lake sediments. In contrast to those diatoms which form a morphologically distinct resistant spore, Melosira is known to produce physiological resting cells that are indistinguishable in outward morphology from actively growing cells.We used both light and electron microscopy to document and elucidate the sequence of cytological changes during the transition from resting cells to actively growing cells in a population of Melosira granulata from Douglas Lake, Michigan sediments collected in mid-July of 1983.

Amorphous silica coating on α-alumina particles

1995 ◽  
Vol 53 ◽  
pp. 210-211
Author(s):  
J. W. Mellowes ◽  
C. M. Chun ◽  
I. A. Aksay
Keyword(s):  
Amorphous Silica ◽  
Heterogeneous Nucleation ◽  
Homogeneous Nucleation ◽  
Silica Coating ◽  
Full Density ◽  
Optimal Conditions ◽  
Fine Grained ◽  
Alumina Particles ◽  
Complete Mullitization ◽  
Powder Compacts

Mullite (3Al2O32SiO2) can be fabricated by transient viscous sintering using composite particles which consist of inner cores of a-alumina and outer coatings of amorphous silica. Powder compacts prepared with these particles are sintered to almost full density at relatively low temperatures (~1300°C) and converted to dense, fine-grained mullite at higher temperatures (>1500°C) by reaction between the alumina core and the silica coating. In order to achieve complete mullitization, optimal conditions for coating alumina particles with amorphous silica must be achieved. Formation of amorphous silica can occur in solution (homogeneous nucleation) or on the surface of alumina (heterogeneous nucleation) depending on the degree of supersaturation of the solvent in which the particles are immersed. Successful coating of silica on alumina occurs when heterogeneous nucleation is promoted and homogeneous nucleation is suppressed. Therefore, one key to successful coating is an understanding of the factors such as pH and concentration that control silica nucleation in aqueous solutions. In the current work, we use TEM to determine the optimal conditions of this processing.

Immunocytochemical methodology for the localization of neuronal antigens at the ultrastructural level

1990 ◽  
Vol 48 (3) ◽  
pp. 876-877
Author(s):  
Jorge Pecci Saavedra ◽  
Mark Connaughton ◽  
Juan José López ◽  
Alicia Brusco
Keyword(s):  
Spinal Cord ◽  
Substantia Nigra ◽  
Polyclonal Antibodies ◽  
Ultrastructural Level ◽  
Point Of View ◽  
Nerve Tissue ◽  
Tissue Fixation ◽  
Optimal Conditions ◽  
Interpeduncular Nucleus ◽  
Technical Point

The use of antibodies as labels for the localization of specific molecules in the nervous systan has been extensively applied in recent years. Both monoand polyclonal antibodies or antisera have been employed. The knowledge of the organization of neuronal connectivities, gliovascular relationships, glioneuronal relationships and other features of nerve tissue has greatly increased.A number of areas of the nervous systan have been analyzed in our laboratory, including the nuclei of the raphe system, the reticular formation, interpeduncular nucleus, substantia nigra, caudate nucleus, putamen, pallidum, spinal cord, pineal gland and others.From a technical point of view, a number of variables needed to be taken into account in order to obtain reliable and reproducible results. The design of the optimal conditions of tissue fixation, embedding, sectioning, dilution of antibodies, and adaptation of Sternberger PAP technique were sane of the parameters taken into account to optimize the results. It is critical that each step of the technique be defined for each particular case.

Substrate specificity and inducibility of TACE (tumour necrosis factor α-converting enzyme) revisited: the Ala-Val preference, and induced intrinsic activity

2003 ◽  
Vol 70 ◽  
pp. 39-52 ◽  
Author(s):  
Roy A. Black ◽  
John R. Doedens ◽  
Rajeev Mahimkar ◽  
Richard Johnson ◽  
Lin Guo ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Recent Work ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Transforming Growth Factor ◽  
Intrinsic Activity ◽  
Converting Enzyme ◽  
Tumour Necrosis Factor Α ◽  
Factor Α ◽  
Necrosis Factor

Tumour necrosis factor α (TNFα)-converting enzyme (TACE/ADAM-17, where ADAM stands for a disintegrin and metalloproteinase) releases from the cell surface the extracellular domains of TNF and several other proteins. Previous studies have found that, while purified TACE preferentially cleaves peptides representing the processing sites in TNF and transforming growth factor α, the cellular enzyme nonetheless also sheds proteins with divergent cleavage sites very efficiently. More recent work, identifying the cleavage site in the p75 TNF receptor, quantifying the susceptibility of additional peptides to cleavage by TACE and identifying additional protein substrates, underlines the complexity of TACE-substrate interactions. In addition to substrate specificity, the mechanism underlying the increased rate of shedding caused by agents that activate cells remains poorly understood. Recent work in this area, utilizing a peptide substrate as a probe for cellular TACE activity, indicates that the intrinsic activity of the enzyme is somehow increased.

Stability of antioxidant vitamins in whole human blood during overnight storage at 4°C and frozen storage up to 6 months

2018 ◽  
Vol 88 (3-4) ◽  
pp. 151-157 ◽  
Author(s):  
Scott W. Leonard ◽  
Gerd Bobe ◽  
Maret G. Traber
Keyword(s):  
Ascorbic Acid ◽  
Whole Blood ◽  
Healthy Subjects ◽  
Frozen Storage ◽  
Blood Collection ◽  
Plasma Samples ◽  
Optimal Conditions ◽  
Plasma Ascorbic Acid ◽  
Blood Samples ◽  
Sample Handling

Abstract. To determine optimal conditions for blood collection during clinical trials, where sample handling logistics might preclude prompt separation of erythrocytes from plasma, healthy subjects (n=8, 6 M/2F) were recruited and non-fasting blood samples were collected into tubes containing different anticoagulants (ethylenediaminetetra-acetic acid (EDTA), Li-heparin or Na-heparin). We hypothesized that heparin, but not EDTA, would effectively protect plasma tocopherols, ascorbic acid, and vitamin E catabolites (α- and γ-CEHC) from oxidative damage. To test this hypothesis, one set of tubes was processed immediately and plasma samples were stored at −80°C, while the other set was stored at 4°C and processed the following morning (~30 hours) and analyzed, or the samples were analyzed after 6 months of storage. Plasma ascorbic acid, as measured using HPLC with electrochemical detection (LC-ECD) decreased by 75% with overnight storage using EDTA as an anticoagulant, but was unchanged when heparin was used. Neither time prior to processing, nor anticoagulant, had any significant effects upon plasma α- or γ-tocopherols or α- or γ-CEHC concentrations. α- and γ-tocopherol concentrations remained unchanged after 6 months of storage at −80°C, when measured using either LC-ECD or LC/mass spectrometry. Thus, refrigeration of whole blood at 4°C overnight does not change plasma α- or γ-tocopherol concentrations or their catabolites. Ascorbic acid is unstable in whole blood when EDTA is used as an anticoagulant, but when whole blood is collected with heparin, it can be stored overnight and subsequently processed.

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