31P Nuclear Magnetic Resonance Evidence for Polyphosphoinositide Associated with the Hydrophobic Segment of Glycophorin A

Ian M. Armitage, Donald L. Shapiro, Heinz Furthmayr, Vincent T. Marchesi

Research output: Contribution to journalArticle

43 Citations (Scopus)

Abstract

Glycophorin A, the major human erythrocyte sialoglycoprotein, contains a significant amount of phosphorus when isolated by the lithium diiodosalicylate-phenol procedure. Only a small percentage (approximately 1%) of this phosphorus is phosphoprotein. 31P nuclear magnetic resonance (NMR) analysis of glycophorin A has identified the remaining phosphorus content as phospholipid in origin. From the 31P chemical shifts, the phospholipid has been identified as diphosphoinositide. 31P NMR spectra of the peptides produced by trypsin hydrolysis of glycophorin A reveal that all the diphosphoinositide is closely associated with the hydrophobic region of the protein, suggesting that there is a specific affinity between this phospholipid and the intramembranous portion of glycophorin A.

Original languageEnglish (US)
Pages (from-to)1317-1320
Number of pages4
JournalBiochemistry
Volume16
Issue number7
DOIs
StatePublished - Apr 1 1977

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Glycophorin
Phosphatidylinositol Phosphates
Magnetic Resonance Spectroscopy
Nuclear magnetic resonance
Phosphorus
Phospholipids
Phosphoproteins
Chemical shift
Phenol
Trypsin
Hydrolysis
Peptides
Proteins

Cite this

31P Nuclear Magnetic Resonance Evidence for Polyphosphoinositide Associated with the Hydrophobic Segment of Glycophorin A. / Armitage, Ian M.; Shapiro, Donald L.; Furthmayr, Heinz; Marchesi, Vincent T.

In: Biochemistry, Vol. 16, No. 7, 01.04.1977, p. 1317-1320.

Research output: Contribution to journalArticle

Armitage, Ian M. ; Shapiro, Donald L. ; Furthmayr, Heinz ; Marchesi, Vincent T. / 31P Nuclear Magnetic Resonance Evidence for Polyphosphoinositide Associated with the Hydrophobic Segment of Glycophorin A. In: Biochemistry. 1977 ; Vol. 16, No. 7. pp. 1317-1320.
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