The toxic effects of benzyl glucosinolate and its hydrolysis product, the biofumigant benzyl isothiocyanate, toFolsomia fimetaria

2010 ◽  
Vol 29 (2) ◽  
pp. 359-364 ◽  
Author(s):  
John Jensen ◽  
Bjarne Styrishave ◽  
Anne Louise Gimsing ◽  
Hans Christian Bruun Hansen
Keyword(s):  
Hydrolysis Product ◽  
Toxic Effects ◽  
Benzyl Isothiocyanate

scholarly journals Characterization of Conjugates between α-Lactalbumin and Benzyl Isothiocyanate—Effects on Molecular Structure and Proteolytic Stability

Molecules ◽  
2021 ◽  
Vol 26 (20) ◽  
pp. 6247
Author(s):  
Jenny Spöttel ◽  
Johannes Brockelt ◽  
Sven Falke ◽  
Sascha Rohn
Keyword(s):  
Molecular Structure ◽  
Hydrolysis Product ◽  
Surface Hydrophobicity ◽  
Biological Properties ◽  
Spectrometric Analysis ◽  
Side Chains ◽  
Plant Metabolites ◽  
Chemical Modifications ◽  
Benzyl Isothiocyanate ◽  
Secondary Plant Metabolites

In complex foods, bioactive secondary plant metabolites (SPM) can bind to food proteins. Especially when being covalently bound, such modifications can alter the structure and, thus, the functional and biological properties of the proteins. Additionally, the bioactivity of the SPM can be affected as well. Consequently, knowledge of the influence of chemical modifications on these properties is particularly important for food processing, food safety, and nutritional physiology. As a model, the molecular structure of conjugates between the bioactive metabolite benzyl isothiocyanate (BITC, a hydrolysis product of the glucosinolate glucotropaeolin) and the whey protein α-lactalbumin (α-LA) was investigated using circular dichroism spectroscopy, anilino-1-naphthalenesulfonic acid fluorescence, and dynamic light scattering. Free amino groups were determined before and after the BITC conjugation. Finally, mass spectrometric analysis of the BITC-α-LA protein hydrolysates was performed. As a result of the chemical modifications, a change in the secondary structure of α-LA and an increase in surface hydrophobicity and hydrodynamic radii were documented. BITC modification at the ε-amino group of certain lysine side chains inhibited tryptic hydrolysis. Furthermore, two BITC-modified amino acids were identified, located at two lysine side chains (K32 and K113) in the amino acid sequence of α-LA.

Mineralization of benzyl glucosinolate and its hydrolysis product the biofumigant benzyl isothiocyanate in soil

2008 ◽  
Vol 40 (1) ◽  
pp. 135-141 ◽  
Author(s):  
Jes Leisgaard Poulsen ◽  
Anne Louise Gimsing ◽  
Barbara Ann Halkier ◽  
Nanna Bjarnholt ◽  
Hans Christian Bruun Hansen
Keyword(s):  
Hydrolysis Product ◽  
Benzyl Isothiocyanate

Ultrastructure of the effect of T-514 obtained from Karwinskia humboldtiana on assembly and integrity of yeast's peroxisomes

1991 ◽  
Vol 49 ◽  
pp. 136-137
Author(s):  
J. Sepulveda-Saavedra ◽  
I. Vander-Klei ◽  
M. Venhuis ◽  
Y. Piñeyro-Lopez
Keyword(s):  
Culture Conditions ◽  
Toxic Effects ◽  
Candida Boidinii ◽  
Central Mexico ◽  
Poisonous Plant ◽  
Biological Behaviour ◽  
Enzyme Content ◽  
Fat Deposits ◽  
Yeast Model

Karwinskia humboldtiana is a poisonous plant that grows in semi desertic areas in north and central México. It produces several substances with different toxic effects. One of them designated T-514 damages severely the lung, kidney and liver, producing in the hepatoeyte large intracellular fat deposits and necrosis. Preliminary observations demonstrated that three is a decrease in the amount of peroxisomes in the hepatocytes of experimentally intoxicated rats and monkeys. To study the effect exerted by the T-514 on peroxisomes, a yeast model was selected, thus, three species: Saccha romices cerevisiae, Ilansenula polymorpha and Candida boidinii were used, because there is information concerning their peroxisome's morphology, enzyme content, biological behaviour under different culture conditions and biogenesis.

Some Conditions Necessary for Pinocytosis

1968 ◽  
Vol 26 ◽  
pp. 142-143
Author(s):  
M. W. Brightman
Keyword(s):  
Smooth Muscle ◽  
Cell Membrane ◽  
Toxic Effects ◽  
Cytological Evidence ◽  
Cell Processes

The cytological evidence for pinocytosis is the focal infolding of the cell membrane to form surface pits that eventually pinch off and move into the cytoplasm. This activity, which can be inhibited by oxidative and glycolytic poisons, is performed only by cell processes that are at least 300A wide. However, the interpretation of such toxic effects becomes equivocal if the membrane invaginations do not normally lead to the formation of migratory vesicles, as in some endothelia and in smooth muscle. The present study is an attempt to set forth some conditions under which pinocytosis, as distinct from the mere inclusion of material in surface invaginations, can take place.

Toxic effects of aerosol propellants on the heart

1973 ◽  
Vol 131 (1) ◽  
pp. 162-166 ◽  
Author(s):  
W. S. Harris
Keyword(s):  
Toxic Effects

Centella asiatica Protects Against the Toxic Effects of Intracellular beta-amyloid Accumulation

Planta Medica ◽  
2013 ◽  
Vol 79 (10) ◽  
Author(s):  
N Gray ◽  
J Morré ◽  
J Kelley ◽  
C Maier ◽  
F Stevens ◽  
...  
Keyword(s):  
Centella Asiatica ◽  
Beta Amyloid ◽  
Toxic Effects ◽  
Amyloid Accumulation

Prostacyclin Synthesis Is Stimulated by a Serum Factor Formed During Coagulation

1983 ◽  
Vol 49 (01) ◽  
pp. 058-060 ◽  
Author(s):  
J M Ritter ◽  
M-A Ongari ◽  
M A Orchard ◽  
P J Lewis
Keyword(s):  
Renal Failure ◽  
Hydrolysis Product ◽  
Healthy Controls ◽  
Serum Factor ◽  
Intrinsic Pathway ◽  
Extrinsic Pathway ◽  
Stimulatory Activity ◽  
Plasma Factor ◽  
Stimulating Factor ◽  
Prostacyclin Synthesis

SummaryFresh aortic rings incubated in serum produce more 6-oxo-PGF1α, the stable hydrolysis product of prostacyclin, than in plasma or buffer. A method is described of recovering this stimulatory activity from a dialysate of serum, showing that the activity is due to a prostacyclin stimulating factor. This factor is formed during coagulation initiated by the intrinsic pathway but not by the extrinsic pathway or by thrombin. By contrast with a previously described plasma factor, the activity of the prostacy-clinstimulating factor in serum is not greater in serum from patients with renal failure than from healthy controls. The stimulating factor is antagonised by heparin, but differs in other ways from previously described platelet derived stimulating factor(s).

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