Prothrombin fragment 1-membrane interactions: a calcium-43 NMR study

Elene Bouhoutsos-Brown; Carol H. Pletcher; Gary L. Nelsestuen; Robert G. Bryant

doi:10.1016/0162-0134(84)85055-2

Prothrombin fragment 1-membrane interactions: a calcium-43 NMR study

Elene Bouhoutsos-Brown, Carol H. Pletcher, Gary L. Nelsestuen, Robert G. Bryant

Metabolic and Systems Biology (BMBB)

Research output: Contribution to journal › Article › peer-review

3 Scopus citations

Abstract

The ⁴³Ca NMR spectra are reported for solutions of prothrombin fragment 1 in the presence and absence of phospholipid. The calcium NMR spectrum permits distinction between three thermodynamic classes of calcium-binding interactions. The calcium ion in the lipid-free solutions was labile, with maximum residence times estimated for the average protein site in the range of 0.5-1 ms. The calcium spectrum was sensitive to the protein association and the addition of phospholipid, which appears to sharpen the calcium specificity for the protein sites. The calcium NMR spectra in the presence of phospholipid are similar to those in lipid-free solutions, which suggests that the calcium ion remains labile in the lipid-protein complex.

Original language	English (US)
Pages (from-to)	337-343
Number of pages	7
Journal	Journal of Inorganic Biochemistry
Volume	21
Issue number	4
DOIs	https://doi.org/10.1016/0162-0134(84)85055-2
State	Published - Aug 1984

Bibliographical note

Funding Information:
This research was supported by the National Institutes of Health, GM-25757 (R.G.B.), HL = I5728 (G.L.N.). and by PostdoctoralF ellowships to C.H.P.. NIH-05927 and to E.B-B.. The Minnesota Heort Association.

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title = "Prothrombin fragment 1-membrane interactions: a calcium-43 NMR study",

abstract = "The 43Ca NMR spectra are reported for solutions of prothrombin fragment 1 in the presence and absence of phospholipid. The calcium NMR spectrum permits distinction between three thermodynamic classes of calcium-binding interactions. The calcium ion in the lipid-free solutions was labile, with maximum residence times estimated for the average protein site in the range of 0.5-1 ms. The calcium spectrum was sensitive to the protein association and the addition of phospholipid, which appears to sharpen the calcium specificity for the protein sites. The calcium NMR spectra in the presence of phospholipid are similar to those in lipid-free solutions, which suggests that the calcium ion remains labile in the lipid-protein complex.",

author = "Elene Bouhoutsos-Brown and Pletcher, {Carol H.} and Nelsestuen, {Gary L.} and Bryant, {Robert G.}",

note = "Funding Information: This research was supported by the National Institutes of Health, GM-25757 (R.G.B.), HL = I5728 (G.L.N.). and by PostdoctoralF ellowships to C.H.P.. NIH-05927 and to E.B-B.. The Minnesota Heort Association.",

year = "1984",

month = aug,

doi = "10.1016/0162-0134(84)85055-2",

language = "English (US)",

volume = "21",

pages = "337--343",

journal = "Journal of Inorganic Biochemistry",

issn = "0162-0134",

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T1 - Prothrombin fragment 1-membrane interactions

T2 - a calcium-43 NMR study

AU - Bouhoutsos-Brown, Elene

AU - Pletcher, Carol H.

AU - Nelsestuen, Gary L.

AU - Bryant, Robert G.

N1 - Funding Information: This research was supported by the National Institutes of Health, GM-25757 (R.G.B.), HL = I5728 (G.L.N.). and by PostdoctoralF ellowships to C.H.P.. NIH-05927 and to E.B-B.. The Minnesota Heort Association.

PY - 1984/8

Y1 - 1984/8

N2 - The 43Ca NMR spectra are reported for solutions of prothrombin fragment 1 in the presence and absence of phospholipid. The calcium NMR spectrum permits distinction between three thermodynamic classes of calcium-binding interactions. The calcium ion in the lipid-free solutions was labile, with maximum residence times estimated for the average protein site in the range of 0.5-1 ms. The calcium spectrum was sensitive to the protein association and the addition of phospholipid, which appears to sharpen the calcium specificity for the protein sites. The calcium NMR spectra in the presence of phospholipid are similar to those in lipid-free solutions, which suggests that the calcium ion remains labile in the lipid-protein complex.

AB - The 43Ca NMR spectra are reported for solutions of prothrombin fragment 1 in the presence and absence of phospholipid. The calcium NMR spectrum permits distinction between three thermodynamic classes of calcium-binding interactions. The calcium ion in the lipid-free solutions was labile, with maximum residence times estimated for the average protein site in the range of 0.5-1 ms. The calcium spectrum was sensitive to the protein association and the addition of phospholipid, which appears to sharpen the calcium specificity for the protein sites. The calcium NMR spectra in the presence of phospholipid are similar to those in lipid-free solutions, which suggests that the calcium ion remains labile in the lipid-protein complex.

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DO - 10.1016/0162-0134(84)85055-2

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AN - SCOPUS:0021171131

VL - 21

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EP - 343

JO - Journal of Inorganic Biochemistry

JF - Journal of Inorganic Biochemistry

SN - 0162-0134

IS - 4

ER -

Prothrombin fragment 1-membrane interactions: a calcium-43 NMR study

Abstract

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