Transbilayer Movement of Phosphatidylserine in Erythrocytes: Inhibition of Transport and Preferential Labeling of a 31 000-Dalton Protein by Sulfhydryl Reactive Reagents

Jerome Connor, Alan J. Schroit

Research output: Contribution to journalArticle

111 Scopus citations

Abstract

A series of labeled thiolation reagents were synthesized on the basis of the parent structure pyridyldithioethylamine (PDA). These compounds specifically and reversibly inhibit the active intrabilayer transport of phosphatidylserine (PS) in human red blood cells. The binding of PDA to cells can be quantified since the thiol-disulfide exchange reaction yields a chromophore. In addition, the presence of a primary amine makes it amenable to derivatization with a variety of compounds. An iodinated derivative of PDA preferentially labeled a 31 000-dalton red blood cell peptide. The labeled component, which may represent the PS transporter, comigrated with integral membrane protein band 7.

Original languageEnglish (US)
Pages (from-to)848-851
Number of pages4
JournalBiochemistry
Volume27
Issue number3
DOIs
StatePublished - Feb 1 1988

ASJC Scopus subject areas

  • Biochemistry

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