Inhibition of mitochondrial phosphate transport by <i>p</i>-diazobenzenesulphonate (<i>Short Communication</i>)

Dawson, Alan P.

doi:10.1042/bj1440597

Cited by 13 publications

(1 citation statement)

References 12 publications

(13 reference statements)

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“…Diazobenzenesulfonate may be particularly useful in elucidating carrier mediated transport since it reacts with a variety of amino acid side chains including those of tryptophan, arginine, histidine, tyrosine, lysine, and cysteine . Mitochondrial phosphate ion uptake, which occurs by a carrier mediated process, has been previously demonstrated to be inhibited by diazobenzenesulfonate (Dawson, 1974).…”

Section: Resultsmentioning

confidence: 99%

Mitochondrial neutral amino acid transport: evidence for a carrier mediated mechanism

Cybulski¹,

Fisher²

1977

Biochemistry

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Swelling of rat liver mitochondria induced by various neutral amino acids indicates that the L isomers of serine, alanine, methionine, valine, threonine, and leucine enter the mitochondrial matrix by a stereospecific process. Chemical modification of mitochondria with diazobenzenesulfonate or p-mercuribenzoate inhibited the rapid uptake of these compounds, as well as that of L-proline and glycine, to various extents. Diazobenzenesulfonate did not inhibit the transport of compounds that enter the mitochondrial matrix by simple diffusion, i.e., thiocyanate, nitrate, formate, bicarbonate, and acetate. Inhibition by p-mercuribenzoate was reversed by treatment with dithiothreitol. Inclusion of various neutral amino acids in the p-mercuribenzoate preincubation mixture substantially prevented inactivation of transport. Glycine, D- or L-serine, L-threonine, L-methionine, L-alanine, and L-valine all individually protected against the inactivation of glycine, L-serine, L-threonine, L-methionine, L-alanine, L-valine, L-proline, and beta-alanine transport, while L-proline, beta-alanine,

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Section: Resultsmentioning

confidence: 99%

Mitochondrial neutral amino acid transport: evidence for a carrier mediated mechanism

Cybulski¹,

Fisher²

1977

Biochemistry

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SH-group reagents as tools in the study of mitochondrial anion transport

Fonyò

1978

J Bioenerg Biomembr

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Phosphate transport in rat liver mitochondria: Location of sulfhydryl groups essential for transport activities

Wehrle

Pedersen

1981

J Bioenerg Biomembr

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The membrane orientation and symmetry of protein thiol group(s) necessary for transport of Pi in rat liver mitochondria have been assessed by comparing inhibition of transport in intact mitochondria to that in inverted vesicles of purified inner membrane. The permeability characteristics of a variety of inhibitors have been determined under specified conditions. The sensitivities of the uptake pathways in mitochondria and in inverted vesicles appear thus far to be identical. By comparing results with permeant and nonpermeant inhibitors, or sequential treatment with different inhibitors, arguments can be made in favor of a single reorienting site of thiol sensitivity.

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Inhibition of mitochondrial phosphate transport by p-diazobenzenesulphonate (Short Communication)

Cited by 13 publications

References 12 publications

Mitochondrial neutral amino acid transport: evidence for a carrier mediated mechanism

Mitochondrial neutral amino acid transport: evidence for a carrier mediated mechanism

SH-group reagents as tools in the study of mitochondrial anion transport

Phosphate transport in rat liver mitochondria: Location of sulfhydryl groups essential for transport activities

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