Afaltoxin B1 transport in rat blood plasma. Binding to albumin in vivo and in vitro and spectrofluorimetric studies into the nature of the interaction

Dirr, Heini W.; Schabort, J.C.

doi:10.1016/0304-4165(86)90030-9

Cited by 25 publications

(14 citation statements)

References 36 publications

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“…The shift of emission maximum to the blue is indicative of the tryptophan microenvironment becoming more hydrophobic. 19 Remission of aflatoxin fluorescence near 430 nm indicates an efficient energy transfer mechanism.…”

Section: Resultsmentioning

confidence: 99%

“…Binding of AFB 1 to various proteins has been reported to aflatoxin b 1 interactions with srp components 11 change their conformations, which possibly affect their functioning. 19 Binding of AFB 1 to rat plasma albumin under in vivo and in vitro conditions was studied by Dirr and Schabort 19 who observed that AFB 1 primarily binds to plasma albumin at an apolar site and only to a limited degree to the other plasma proteins. Chi'h and Devlin 27 have reported that the binding ability of AFB 1 to histones is quite low.…”

Section: Resultsmentioning

confidence: 99%

“…Spectrofluorimetric studies of AFB 1 -polypeptide complexes (Figures 2 and 3) were carried out as described above for dog pancreatic SRP according to the method of Dirr and Schabort. 19 …”

mentioning

confidence: 97%

“…The SRP preparation (equivalent to 1 mg ml À1 protein) was incubated with a 15-mM solution of freshly synthesized aflatoxin B 1 -8, 9-epoxide (AFB 1 epoxide) at 37 C for 90 min in a reaction volume of 100 ml. Unbound epoxide was extracted thrice with diethyl ether and spectrofluorimetric study of the SRP-AFB 1 complex was undertaken using the method of Dirr and Schabort 19 with excitation at 295 nm and emission at 340 nm ( Figure 1). Band widths for excitation and emission were 4 and 6 nm respectively.…”

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confidence: 99%

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Interactions of aflatoxin B1 with SRP components can disrupt protein targeting

Singh

Dani

et al. 2004

Cell Biochem. Funct.

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Spectrofluorimetric studies have revealed that aflatoxin B1 (AFB1) interacts with signal recognition particle (SRP), which acts as an escort for polyribosomes with signal peptides to be transported and bound to the cytoplasmic face of the endoplasmic reticulum (ER). We further report that the binding of AFB1 to SRP is selective as it only binds to two (SRP9 and 14) out of its three constituent polypeptides studied. Binding of AFB1 to proteins is known to alter their conformations. Interactions of AFB1 with SRP polypeptides may generate structural and functional alterations in this particle and hinder secretory protein synthesis.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

“…Spectrofluorimetric studies of AFB 1 -polypeptide complexes (Figures 2 and 3) were carried out as described above for dog pancreatic SRP according to the method of Dirr and Schabort. 19 …”

mentioning

confidence: 97%

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confidence: 99%

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Interactions of aflatoxin B1 with SRP components can disrupt protein targeting

Singh

Dani

et al. 2004

Cell Biochem. Funct.

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“…Compared with the free animal cells, immobilized rat erythrocytes were temperature resistant. Dirr and Schabort (1986) revealed the mechanism of transport of AFB 1 in rat blood plasma binding of AFB 1 to albumin in vivo and in vitro and performed spectroflurimetric studies of the nature of interaction of these macromolecules to AFB 1 . In 1987 they characterized the AFB 1 binding site in rat albumin.…”

Section: B Nuclear Metabolismmentioning

confidence: 99%

A Review on Biological Control and Metabolism of Aflatoxin

Mishra¹,

Das²

2003

Critical Reviews in Food Science and Nutrition

249

135

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The series of events that led to the discovery of aflatoxin as a potent carcinogen, its biosynthesis, mechanism of action, structure-function relationship provide interesting insight into the economical and technological factors involved in the development of an effective control measure for the toxin. Scientists all over the world are making continuous efforts to explore a generalized process of detoxification, which can bring down the toxin content in heterogenous commodities to a threshold level. In this article biological control methods with special emphasis on in vivo and in vitro enzymatic detoxification of aflatoxin have been reviewed. Future areas of research involving large-scale enzymatic detoxification and modified atmosphere storage are also discussed.

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ADMEof Natural Toxins

González‐Pérez

Kroll

2012

Encyclopedia of Drug Metabolism and Interactions

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A common myth among the general public is that any substance derived from nature is inherently safe. To the contrary, some of the most potent and specifically‐targeted toxins have been identified and isolated from plants, mushrooms, and microorganisms. With regard to this volume, many of these toxins are of particular relevance in the pharmacokinetic study of xenobiotics, particularly their metabolism. This chapter highlights a select group of primarily small molecule toxins or protoxins of historical (i.e., aflatoxins) or contemporary (i.e., mycotoxins from “toxic mold”) relevance. Marine peptide toxins are intentionally omitted to maintain focus but are an additional class of highly‐selective acute and potentially lethal toxins from nature.

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Afaltoxin B1 transport in rat blood plasma. Binding to albumin in vivo and in vitro and spectrofluorimetric studies into the nature of the interaction

Cited by 25 publications

References 36 publications

Interactions of aflatoxin B1 with SRP components can disrupt protein targeting

Interactions of aflatoxin B1 with SRP components can disrupt protein targeting

A Review on Biological Control and Metabolism of Aflatoxin

ADMEof Natural Toxins

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