Leucine enkephalin-tyrosinase reaction products - Identification and biological activity

Véronique Larsimont; Laszlo Prokai; Günther Hochhaus

doi:10.1016/0167-4889(94)90029-9

Leucine enkephalin-tyrosinase reaction products - Identification and biological activity

Véronique Larsimont, Laszlo Prokai, Günther Hochhaus

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Abstract

Leucine enkephalin (1 mM) was reacted with mushroom tyrosinase under reductive conditions (ascorbic acid, 50 mM). Reaction products were isolated by high-performance liquid chromatography and identified using electrospray ionization mass spectrometry. The products of the reaction were found to be hydroxylated at the Tyr¹ moiety of the peptide. The major product was a monohydroxylated derivative of leucine enkephalin ([HO-Tyr¹]LE) and the minor product of the reaction was a dihydroxylated derivative ([(HO)₂-Tyr¹]LE). The affinity of [HO-Tyr¹]LE to receptors in rat brain homogenate was compared to that of leucine enkephalin itself. Hydroxylation of LE was found to decrease receptor affinity to both μ and δ opioid receptor sites by a factor of about 20.

Original language	English
Pages (from-to)	95-100
Number of pages	6
Journal	BBA - Molecular Cell Research
Volume	1222
Issue number	1
DOIs	https://doi.org/10.1016/0167-4889(94)90029-9
State	Published - 26 May 1994

Keywords

Enkephalin
Mass spectrometry
Receptor affinity
Tyrosinase

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10.1016/0167-4889(94)90029-9

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@article{c572f9bc1e834ad4971cd8b3b542c4b5,

title = "Leucine enkephalin-tyrosinase reaction products - Identification and biological activity",

abstract = "Leucine enkephalin (1 mM) was reacted with mushroom tyrosinase under reductive conditions (ascorbic acid, 50 mM). Reaction products were isolated by high-performance liquid chromatography and identified using electrospray ionization mass spectrometry. The products of the reaction were found to be hydroxylated at the Tyr1 moiety of the peptide. The major product was a monohydroxylated derivative of leucine enkephalin ([HO-Tyr1]LE) and the minor product of the reaction was a dihydroxylated derivative ([(HO)2-Tyr1]LE). The affinity of [HO-Tyr1]LE to receptors in rat brain homogenate was compared to that of leucine enkephalin itself. Hydroxylation of LE was found to decrease receptor affinity to both μ and δ opioid receptor sites by a factor of about 20.",

keywords = "Enkephalin, Mass spectrometry, Receptor affinity, Tyrosinase",

author = "V{\'e}ronique Larsimont and Laszlo Prokai and G{\"u}nther Hochhaus",

note = "Funding Information: This work was supported by a PDA Foundation and Schering-Plough Corporation Foundation Grant in Biotechnology.",

year = "1994",

month = may,

day = "26",

doi = "10.1016/0167-4889(94)90029-9",

language = "English",

volume = "1222",

pages = "95--100",

journal = "BBA - Molecular Cell Research",

issn = "0167-4889",

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TY - JOUR

T1 - Leucine enkephalin-tyrosinase reaction products - Identification and biological activity

AU - Larsimont, Véronique

AU - Prokai, Laszlo

AU - Hochhaus, Günther

N1 - Funding Information: This work was supported by a PDA Foundation and Schering-Plough Corporation Foundation Grant in Biotechnology.

PY - 1994/5/26

Y1 - 1994/5/26

N2 - Leucine enkephalin (1 mM) was reacted with mushroom tyrosinase under reductive conditions (ascorbic acid, 50 mM). Reaction products were isolated by high-performance liquid chromatography and identified using electrospray ionization mass spectrometry. The products of the reaction were found to be hydroxylated at the Tyr1 moiety of the peptide. The major product was a monohydroxylated derivative of leucine enkephalin ([HO-Tyr1]LE) and the minor product of the reaction was a dihydroxylated derivative ([(HO)2-Tyr1]LE). The affinity of [HO-Tyr1]LE to receptors in rat brain homogenate was compared to that of leucine enkephalin itself. Hydroxylation of LE was found to decrease receptor affinity to both μ and δ opioid receptor sites by a factor of about 20.

AB - Leucine enkephalin (1 mM) was reacted with mushroom tyrosinase under reductive conditions (ascorbic acid, 50 mM). Reaction products were isolated by high-performance liquid chromatography and identified using electrospray ionization mass spectrometry. The products of the reaction were found to be hydroxylated at the Tyr1 moiety of the peptide. The major product was a monohydroxylated derivative of leucine enkephalin ([HO-Tyr1]LE) and the minor product of the reaction was a dihydroxylated derivative ([(HO)2-Tyr1]LE). The affinity of [HO-Tyr1]LE to receptors in rat brain homogenate was compared to that of leucine enkephalin itself. Hydroxylation of LE was found to decrease receptor affinity to both μ and δ opioid receptor sites by a factor of about 20.

KW - Enkephalin

KW - Mass spectrometry

KW - Receptor affinity

KW - Tyrosinase

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U2 - 10.1016/0167-4889(94)90029-9

DO - 10.1016/0167-4889(94)90029-9

M3 - Article

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AN - SCOPUS:0028352668

SN - 0167-4889

VL - 1222

SP - 95

EP - 100

JO - BBA - Molecular Cell Research

JF - BBA - Molecular Cell Research

IS - 1

ER -

Leucine enkephalin-tyrosinase reaction products - Identification and biological activity

Abstract

Keywords

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