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THE ACTION OF SODIUM DODECYL SULFATE ON THE CHLOROPHYLL-PROTEIN COMPOUND OF THE SPINACH LEAF

1. Sodium dodecyl sulfate (SDS) attacks the chlorophyll-protein compound modifying its protein properties and absorption spectrum. 2. In the presence of SDS, chlorophyll is quantitatively converted to phaeophytin; i.e., magnesium is removed from the molecule. This reaction, measured spectrophotometr...

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Autor principal: Smith, Emil L.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1941
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2237990/
https://www.ncbi.nlm.nih.gov/pubmed/19873236
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author Smith, Emil L.
author_facet Smith, Emil L.
author_sort Smith, Emil L.
collection PubMed
description 1. Sodium dodecyl sulfate (SDS) attacks the chlorophyll-protein compound modifying its protein properties and absorption spectrum. 2. In the presence of SDS, chlorophyll is quantitatively converted to phaeophytin; i.e., magnesium is removed from the molecule. This reaction, measured spectrophotometrically, proceeds at a rate directly proportional to the hydrogen ion concentration. At constant pH, the rate is proportional to the SDS concentration until a maximum rate is achieved. 3. The chlorophyll or phaeophytin (depending on the pH) remains attached to the protein, since the prosthetic group cannot be separated by ultrafiltration, dialysis, or fractional precipitation. 4. This suggests that the magnesium plays no part in binding chlorophyll to the split protein fragments, but may be concerned in binding the larger units, since the metal becomes extremely labile when the protein is split.
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spelling pubmed-22379902008-04-23 THE ACTION OF SODIUM DODECYL SULFATE ON THE CHLOROPHYLL-PROTEIN COMPOUND OF THE SPINACH LEAF Smith, Emil L. J Gen Physiol Article 1. Sodium dodecyl sulfate (SDS) attacks the chlorophyll-protein compound modifying its protein properties and absorption spectrum. 2. In the presence of SDS, chlorophyll is quantitatively converted to phaeophytin; i.e., magnesium is removed from the molecule. This reaction, measured spectrophotometrically, proceeds at a rate directly proportional to the hydrogen ion concentration. At constant pH, the rate is proportional to the SDS concentration until a maximum rate is achieved. 3. The chlorophyll or phaeophytin (depending on the pH) remains attached to the protein, since the prosthetic group cannot be separated by ultrafiltration, dialysis, or fractional precipitation. 4. This suggests that the magnesium plays no part in binding chlorophyll to the split protein fragments, but may be concerned in binding the larger units, since the metal becomes extremely labile when the protein is split. The Rockefeller University Press 1941-05-20 /pmc/articles/PMC2237990/ /pubmed/19873236 Text en Copyright © Copyright, 1941, by The Rockefeller Institute for Medical Research This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Article
Smith, Emil L.
THE ACTION OF SODIUM DODECYL SULFATE ON THE CHLOROPHYLL-PROTEIN COMPOUND OF THE SPINACH LEAF
title THE ACTION OF SODIUM DODECYL SULFATE ON THE CHLOROPHYLL-PROTEIN COMPOUND OF THE SPINACH LEAF
title_full THE ACTION OF SODIUM DODECYL SULFATE ON THE CHLOROPHYLL-PROTEIN COMPOUND OF THE SPINACH LEAF
title_fullStr THE ACTION OF SODIUM DODECYL SULFATE ON THE CHLOROPHYLL-PROTEIN COMPOUND OF THE SPINACH LEAF
title_full_unstemmed THE ACTION OF SODIUM DODECYL SULFATE ON THE CHLOROPHYLL-PROTEIN COMPOUND OF THE SPINACH LEAF
title_short THE ACTION OF SODIUM DODECYL SULFATE ON THE CHLOROPHYLL-PROTEIN COMPOUND OF THE SPINACH LEAF
title_sort action of sodium dodecyl sulfate on the chlorophyll-protein compound of the spinach leaf
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2237990/
https://www.ncbi.nlm.nih.gov/pubmed/19873236
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