What question did this study set out to answer?

To synthesize and characterize N-hydroxysulfosuccinimide and develop water-soluble, membrane-impermeant reagents for selective protein cross-linking under physiological conditions.

August 17, 1982Biochemistry

N-hydroxysulfosuccinimide active esters: bis(N-hydroxysulfosuccinimide) esters of two dicarboxylic acids are hydrophilic, membrane-impermeant, protein cross-linkers

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Authors

JSJames V. StarosUniversity of Massachusetts Amherst

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Overview

In vitro study demonstrates hydrophilic active esters achieve selective surface protein cross-linking in human erythrocytes, indicating their utility as membrane-impermeant molecular probes.

Key Points

To synthesize and characterize N-hydroxysulfosuccinimide and develop water-soluble, membrane-impermeant reagents for selective protein cross-linking under physiological conditions.
Synthesized N-hydroxysulfosuccinimide and incorporated it into two cross-linking reagents: 3,3'-dithiobis(sulfosuccinimidyl propionate) and bis(sulfosuccinimidyl) suberate.
Assayed cross-linking efficiency and chemical cleavability using rabbit muscle aldolase at physiological pH.
Evaluated membrane permeability and surface protein cross-linking in intact human erythrocytes and isolated erythrocyte membranes.
Both reagents acted as highly efficient protein cross-linkers at physiological pH, with 3,3'-dithiobis(sulfosuccinimidyl propionate) demonstrating quantitative cleavage upon mild reduction.
Both cross-linkers proved completely membrane-impermeant in intact human erythrocytes, selectively cross-linking band 3 anion channel subunits into covalent dimers at the external membrane surface.

Cite This Study

James V. Staros (1982) studied this question.

synapsesocial.com/papers/6a7299d5f44fa9f079e004fd https://doi.org/10.1021/bi00260a008

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August 17, 1982Biochemistry

N-hydroxysulfosuccinimide active esters: bis(N-hydroxysulfosuccinimide) esters of two dicarboxylic acids are hydrophilic, membrane-impermeant, protein cross-linkers

View Full Paper

Ask AI

Bookmark

Authors

JSJames V. StarosUniversity of Massachusetts Amherst

Discussion

Member takes

Overview

In vitro study demonstrates hydrophilic active esters achieve selective surface protein cross-linking in human erythrocytes, indicating their utility as membrane-impermeant molecular probes.

Key Points

To synthesize and characterize N-hydroxysulfosuccinimide and develop water-soluble, membrane-impermeant reagents for selective protein cross-linking under physiological conditions.
Synthesized N-hydroxysulfosuccinimide and incorporated it into two cross-linking reagents: 3,3'-dithiobis(sulfosuccinimidyl propionate) and bis(sulfosuccinimidyl) suberate.
Assayed cross-linking efficiency and chemical cleavability using rabbit muscle aldolase at physiological pH.
Evaluated membrane permeability and surface protein cross-linking in intact human erythrocytes and isolated erythrocyte membranes.
Both reagents acted as highly efficient protein cross-linkers at physiological pH, with 3,3'-dithiobis(sulfosuccinimidyl propionate) demonstrating quantitative cleavage upon mild reduction.
Both cross-linkers proved completely membrane-impermeant in intact human erythrocytes, selectively cross-linking band 3 anion channel subunits into covalent dimers at the external membrane surface.

Cite This Study

James V. Staros (1982) studied this question.

synapsesocial.com/papers/6a7299d5f44fa9f079e004fd https://doi.org/10.1021/bi00260a008

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