Study of folch-pi apoprotein I. Isolation of two components, aggregation during delipidation

Nicot, C.; Le, Trang; Leprêtre, M.; Alfsen, Annette

doi:10.1016/0005-2795(73)90181-5

Cited by 69 publications

(35 citation statements)

References 31 publications

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“…Fur-thermore, this increase was in large measure (but not entirely) due to the accumulation of two proteolipid proteins with apparent molecular weights of 21,500 and 26,000, which agrees well with similar studies performed on mouse brain (Nicot et al, 1973;Lerner et al, 1974). Authentic rat myelin proteolipid protein was found to coelectrophorese with the 26,000 mol wt component from whole brain.…”

Section: Discussionsupporting

confidence: 87%

A regional study of developing rat brain: The accumulation and distribution of proteolipid proteins

Campagnoni

Dutton

et al. 1976

J. Neurobiol.

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The accumulation and distribution of proteolipid proteins in rat brain and selected brain regions (cerebellum, cerebral cortex, basal ganglia, and hippocampus) were studied during early postnatal development. In whole brain an eightfold increase of proteolipid was observed between ten and 33 days after birth. This was reflected in the separate regions examined where the proteolipid protein content increased six- to ten-fold during the same period. The basal ganglia and cerebral cortex contributed the greatest amount to the total proteolipid present. However, at 28-33 days the greatest concentration (mg/g tissue) was observed in the basal ganglia and hippocampus. When the proteolipid protein preparations were examined by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis, distinctive, heterogeneous patterns for each brain region were obtained. Proteolipid from basal ganglia (the region richest in white matter) consisted primarily of two major protein bands with apparent molecular weights of approximately 21,500 and 26,000. Both of these bands dramatically increased in quantity during myelination, and the larger protein coelectrophoresed with isolated myelin proteolipid protein. Both bands were also found present in proteolipid preparations from the other brain regions but in varying amounts relative to the total. The data suggest that the increase in proteolipid observed during this developmental period was due in large measure to the accumulation of myelin-specific proteolipids, but also that a significant proportion of the increase was due to the accumulation of nonmyelin components.

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Section: Discussionsupporting

confidence: 87%

A regional study of developing rat brain: The accumulation and distribution of proteolipid proteins

Campagnoni

Dutton

et al. 1976

J. Neurobiol.

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“…In dissociating conditions (dodecyl sulfate, formic acid) molecular weights ranging from 24000 to 28000 are found [4] in agreement with the value suggested by sequence studies [lO,ll]. In aqueous solution, depending on the experimental conditions, molecular weight values from 79000 to 500000 have been found [4,12].…”

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confidence: 76%

“…ACcording to Cohn and Edsall [15], a value of 0.75 cm3/g can be calculated from the amino-acid analysis [7]. However the presence of a small fraction of components other than amino acid residues is still observed in the Folch-Pi apoprotein after delipidation : 3 -4% (w/w) of fatty acids (Stoffyn [16], Gagnon [17]), cerebrosides corresponding to a minimum of 0.7% (w/w) of galactose and 0.05 % (w/w) of phosphorus assigned to bound phospholipids [12]. Taking into account these components, a specific volume of 0.77 cm3/g is calculated.…”

Section: Partial Specijic Volumementioning

confidence: 99%

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The Molecular Size and Shape of the Folch‐Pi Apoprotein in Aqueous and Organic Solvents

Lavialle

Foresta

Vacher

et al. 1979

European Journal of Biochemistry

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In 1 % acetic acid, sedimentation velocity measurements and equilibrium ultracentrifuge experiments demonstrate that the Folch-Pi apoprotein is not monodisperse. The weight-average molecular weight calculated from ultracentrifuge experiments and combining sedimentation coefficient and viscosity measurements, ranged from 64000 to 80000. The intrinsic viscosity value suggests an asymetric shape for the apoprotein if a low value of hydration is considered.In dioxan/lx acetic acid (2: 3, v/v) a smaller sedimentation coefficient was found, the intrinsic viscosity value remaining identical to that in 1 % acetic acid.

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“…Spontaneous formation of disulfide bridges occurs upon exposure of cysteyl residues to air, as has been characterized in detail for erythrocyte anion exchange protein (Rao, 1979). A number of free sulfhydryles do disappear during PLP purification, presumably due to oxidation (Lees, Leston & Marfey, 1969;Nicot et al, 1973;Cockle et al, 1980). It is therefore probable that some of the disulfide bridges found in the purified peptides do not exist in vivo.…”

Section: Disulfide Bridgesmentioning

confidence: 93%

Major myelin proteolipid: The 4-α-helix topology

1991

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Several conflicting models have been proposed for the membrane arrangement of the major myelin proteolipid (PLP). We have compared features of the sequence of PLP with those of other eukaryotic integral membrane proteins, with the view of identifying the most likely transmembrane topology. A new, simple model is suggested, which features four hydrophobic alpha-helices spanning the whole thickness of the lipid bilayer. Its orientation may be such that both the N- and C-termini face the cytosol. None of the biochemical, biophysical or immunological experiments hitherto reported provides incontrovertible evidence against the model. The effect or absence thereof of various PLP mutations is discussed in the frame of the proposed 4-helix topology.

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Study of folch-pi apoprotein I. Isolation of two components, aggregation during delipidation

Cited by 69 publications

References 31 publications

A regional study of developing rat brain: The accumulation and distribution of proteolipid proteins

A regional study of developing rat brain: The accumulation and distribution of proteolipid proteins

The Molecular Size and Shape of the Folch‐Pi Apoprotein in Aqueous and Organic Solvents

Major myelin proteolipid: The 4-α-helix topology

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