Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Both the MN-glycoprotein from human erythrocytes and the hydrophobic fragment from the protein isolated with trypsin treatment, T(is), have been recombined with egg phosphatidylcholine in bilayers at various phospholipid/protein ratios. In order to investigate the effect of the protein on the phospholipid headgroups, 31P nuclear magnetic resonance spectra were obtained with the MN-glycoprotein recombined with egg phosphatidylcholine, which revealed two classes of phospholipid environments, one immobilized and one not immobilized. Electron spin resonance (ESR) of fatty acid methyl ester spin labels provided supporting evidence. Computer analysis of the ESR spectra indicate that 4-5 moles of phospholipid are immobilized per mole of protein over a wide range of lipid-to-protein ratios. The immobilization of the phospholipids appears mediated by both the polar headgroups and the hydrocarbon tails of the phospholipid.
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PMID:Interaction between glycophorin and phospholipids in recombined systems. 22 68

The membrane-penetrating segment of the surface MN-glycoprotein of the human erythrocyte is contained intact within the tryptic peptide T(is). We report here on the association of this peptide with hydrated phospholipid vesicles. Under these conditions 80 A intramembranous particles, as seen by freeze-etch electron microscopy, are produced that are similar in size to those seen in the native erythrocyte membrane. These particles increase in number as a linear function of T(is) concentration and a plot of particle number versus concentration is compatible with a micelle-like phenomenon; from this curve the critical concentration for the formation of particles is estimated to be approximately one mole of T(is) to 120 moles of lecithin. These data suggest that the membrane-penetrating peptide T(is) is being incorporated, monomerically and multimerically, within the hydrocarbon phase of lecithin bilayers. From these data it can be calculated that each intramembranous particle contains between 10 and 20 T(is) monomers. The peptide portion of each particle, therefore, has a molecular weight of 45,000-85,000. An exact analogy cannot be drawn at this time between the in vivo structure of erythrocyte intramembranous particles and the reconstituted particles described here, although an argument has been constructed to support this possibility. What is clear is that the reconstituted system promises to be useful for further examination of protein-lipid interactions in membranes.
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PMID:Association of the membrane-penetrating polypeptide segment of the human erythrocyte MN-glycoprotein with phospholipid bilayers. I. Formation of freeze-etch intramembranous particles. 452 33