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Article

Native disulfide bonds in plasma retinol-binding protein are not essential for all-trans-retinol-binding activity.

Journal of proteome research - 1 Jan 2000

Reznik Gabriel O, Yu Yong, Tarr George E, Cantor Charles R

Abstract excerpt

A human plasma retinol-binding protein (RBP) mutant, named RBP-S, has been designed and produced in which the six native cysteine residues, involved in the formation of three disulfide bonds, have been replaced with serine. A hexa-histidine tag was also added to the C-terminus of RBP for ease of purification. The removal of the disulfide bonds led to a decrease in the affinity of RBP for all trans-retinol. Data...

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PMID: 12814263
DOI: 10.1021/pr0255809

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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