Interaction of Apolipoprotein-Alanine and Apolipoprotein-Glutamine-I with Phosphatidylcholine. Effect on Solute Quenching of Intrinsic Fluorescence

Henry J. Pownall; Louis C. Smith

doi:10.1021/bi00709a018

Interaction of Apolipoprotein-Alanine and Apolipoprotein-Glutamine-I with Phosphatidylcholine. Effect on Solute Quenching of Intrinsic Fluorescence

Henry J. Pownall, Louis C. Smith

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Abstract

The interaction of egg phosphatidylcholine with apoLP-alanine₁, apoLP-glutamine-I, and human serum albumin has been investigated by quenching of the intrinsic protein fluorescence in both the presence and absence of the phospholipid. The quenching by a negatively charged quencher, iodide ion, used in conjunction with a positively charged quencher, pyridinium ion, reflected the relative charge in the region of tryptophans in the protein and indicated the magnitude of binding of phospholipid. Expressions were derived to quantitate both protein accessibility and the phospholipid binding efficiency of these proteins. ApoLP-alanine₁ bound phospholipid more efficiently than apoLP-glutamine-I. Both apolipoproteins were more efficient than human serum albumin.

Original language	English (US)
Pages (from-to)	2590-2593
Number of pages	4
Journal	Biochemistry
Volume	13
Issue number	12
DOIs	https://doi.org/10.1021/bi00709a018
State	Published - Jun 1 1974

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Biochemistry

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title = "Interaction of Apolipoprotein-Alanine and Apolipoprotein-Glutamine-I with Phosphatidylcholine. Effect on Solute Quenching of Intrinsic Fluorescence",

abstract = "The interaction of egg phosphatidylcholine with apoLP-alanine1, apoLP-glutamine-I, and human serum albumin has been investigated by quenching of the intrinsic protein fluorescence in both the presence and absence of the phospholipid. The quenching by a negatively charged quencher, iodide ion, used in conjunction with a positively charged quencher, pyridinium ion, reflected the relative charge in the region of tryptophans in the protein and indicated the magnitude of binding of phospholipid. Expressions were derived to quantitate both protein accessibility and the phospholipid binding efficiency of these proteins. ApoLP-alanine1 bound phospholipid more efficiently than apoLP-glutamine-I. Both apolipoproteins were more efficient than human serum albumin.",

author = "Pownall, {Henry J.} and Smith, {Louis C.}",

year = "1974",

month = jun,

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doi = "10.1021/bi00709a018",

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journal = "Biochemistry",

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T1 - Interaction of Apolipoprotein-Alanine and Apolipoprotein-Glutamine-I with Phosphatidylcholine. Effect on Solute Quenching of Intrinsic Fluorescence

AU - Pownall, Henry J.

AU - Smith, Louis C.

PY - 1974/6/1

Y1 - 1974/6/1

N2 - The interaction of egg phosphatidylcholine with apoLP-alanine1, apoLP-glutamine-I, and human serum albumin has been investigated by quenching of the intrinsic protein fluorescence in both the presence and absence of the phospholipid. The quenching by a negatively charged quencher, iodide ion, used in conjunction with a positively charged quencher, pyridinium ion, reflected the relative charge in the region of tryptophans in the protein and indicated the magnitude of binding of phospholipid. Expressions were derived to quantitate both protein accessibility and the phospholipid binding efficiency of these proteins. ApoLP-alanine1 bound phospholipid more efficiently than apoLP-glutamine-I. Both apolipoproteins were more efficient than human serum albumin.

AB - The interaction of egg phosphatidylcholine with apoLP-alanine1, apoLP-glutamine-I, and human serum albumin has been investigated by quenching of the intrinsic protein fluorescence in both the presence and absence of the phospholipid. The quenching by a negatively charged quencher, iodide ion, used in conjunction with a positively charged quencher, pyridinium ion, reflected the relative charge in the region of tryptophans in the protein and indicated the magnitude of binding of phospholipid. Expressions were derived to quantitate both protein accessibility and the phospholipid binding efficiency of these proteins. ApoLP-alanine1 bound phospholipid more efficiently than apoLP-glutamine-I. Both apolipoproteins were more efficient than human serum albumin.

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DO - 10.1021/bi00709a018

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JF - Biochemistry

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ER -

Interaction of Apolipoprotein-Alanine and Apolipoprotein-Glutamine-I with Phosphatidylcholine. Effect on Solute Quenching of Intrinsic Fluorescence

Abstract

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