Lysosomal membrane labilization by DDT, DDE and polychlorinated biphenyls (PCB)

A. Rogers; A. Mellors; S. Safe

Lysosomal membrane labilization by DDT, DDE and polychlorinated biphenyls (PCB)

A. Rogers, A. Mellors, S. Safe

Research output: Contribution to journal › Article › peer-review

Abstract

Incubation of the ubiquitous pollutants, polychlorinated biphenyls (PCB), DDT and DDE with rat liver lysosomes shows that these lipophilic substrates are highly active labilizers of lysosomal membranes. The release of acid phosphatase was used as a marker enzyme and at high PCB, DDT and DDE concentrations (2x10^-3M) the lytic activity was similar to that of the detergent Triton X 100; at lower concentrations most of the commercial PCB samples, DDT and DDE still retain considerable lytic activity.

Original language	English (US)
Pages (from-to)	341-344
Number of pages	4
Journal	Research Communications in Chemical Pathology and Pharmacology
Volume	13
Issue number	2
State	Published - 1976

ASJC Scopus subject areas

Pathology and Forensic Medicine
Toxicology
Pharmacology
Pharmacology, Toxicology and Pharmaceutics(all)

Cite this

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abstract = "Incubation of the ubiquitous pollutants, polychlorinated biphenyls (PCB), DDT and DDE with rat liver lysosomes shows that these lipophilic substrates are highly active labilizers of lysosomal membranes. The release of acid phosphatase was used as a marker enzyme and at high PCB, DDT and DDE concentrations (2x10-3M) the lytic activity was similar to that of the detergent Triton X 100; at lower concentrations most of the commercial PCB samples, DDT and DDE still retain considerable lytic activity.",

author = "A. Rogers and A. Mellors and S. Safe",

year = "1976",

language = "English (US)",

volume = "13",

pages = "341--344",

journal = "Research Communications in Chemical Pathology and Pharmacology",

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AU - Rogers, A.

AU - Mellors, A.

AU - Safe, S.

PY - 1976

Y1 - 1976

N2 - Incubation of the ubiquitous pollutants, polychlorinated biphenyls (PCB), DDT and DDE with rat liver lysosomes shows that these lipophilic substrates are highly active labilizers of lysosomal membranes. The release of acid phosphatase was used as a marker enzyme and at high PCB, DDT and DDE concentrations (2x10-3M) the lytic activity was similar to that of the detergent Triton X 100; at lower concentrations most of the commercial PCB samples, DDT and DDE still retain considerable lytic activity.

AB - Incubation of the ubiquitous pollutants, polychlorinated biphenyls (PCB), DDT and DDE with rat liver lysosomes shows that these lipophilic substrates are highly active labilizers of lysosomal membranes. The release of acid phosphatase was used as a marker enzyme and at high PCB, DDT and DDE concentrations (2x10-3M) the lytic activity was similar to that of the detergent Triton X 100; at lower concentrations most of the commercial PCB samples, DDT and DDE still retain considerable lytic activity.

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AN - SCOPUS:0017283107

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JF - Research Communications in Chemical Pathology and Pharmacology

IS - 2

ER -

Lysosomal membrane labilization by DDT, DDE and polychlorinated biphenyls (PCB)

Abstract

ASJC Scopus subject areas

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