Photolabile ligands for opiate receptors

Zioudrou, Christine; Varoucha, D.; Loukas, Spyros; Streaty, Richard A.; Klee, Werner A.

doi:10.1016/0024-3205(82)90182-5

Cited by 14 publications

(7 citation statements)

References 9 publications

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“…These peptides possessed agonist activity in the GPI, but photoactivation was not possible because ultraviolet irradiation alone eliminated completely and irreversibly the electrically stimu lated contractions of the GPI. Recently, two other photoaffinity labels (6, 7) that contain a 2-nitro-4-azidophenyl group linked to [D-Ala 2 ,Leu s ]enkephalin by ethylenediamine or ethylenediamine-�-alanine spacers have been described (48,49). Both compounds had high affinity in displacing [3H]DAME from rat brain membranes, in inhibiting contractions of the MVD, and in inhibiting opiate-sensitive adenylate cyclase of NO 108-15 hybrid cell membranes.…”

Section: Photoaffinity Labelsmentioning

confidence: 99%

Affinity Labels for Opioid Receptors

Takemori

Portoghese

1985

Annu. Rev. Pharmacol. Toxicol.

103

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Section: Photoaffinity Labelsmentioning

confidence: 99%

Affinity Labels for Opioid Receptors

Takemori

Portoghese

1985

Annu. Rev. Pharmacol. Toxicol.

103

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“…Recently, peptides exibiting biological activities such as antihypertensive [2], antimicrobial [3] or opioid [4] activities were isolated in hydrolysates of proteins, increasing the interest of enzymic proteolysis. Numerous peptides showing an opioid‐like activity were isolated from hydrolysates of a wide range of animal or vegetable food protein such as β‐casein [5], wheat gluten [6], soya proteins [7], whey protein [8] or spinach RuBisCO (ribulose bisphosphate carboxylase/oxygenase) [9]. These new kinds of peptides were termed ‘exorphins’, in order to contrast them with the ‘endorphins’ released in vivo from endogenous precursors [10].…”

Section: Introductionmentioning

confidence: 99%

Continuous production of a peptidic fraction containing the intermediate opioid peptide LVV‐haemorphin‐7 (LVVh‐7) by peptic hydrolysis of bovine haemoglobin in a continuous membrane reactor

Kapel¹,

Froidevaux²,

Nedjar‐Arroume³

et al. 2003

Biotech and App Biochem

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Peptic hydrolysis of native bovine haemoglobin at pH 3 yields the LVV-haemorphin-7 (Leu-Val-Val-Tyr-Pro-Trp-Thr-Gln-Arg-Phe; LVVh-7) opioid peptide corresponding to the residues-31-40 fragment of the beta-chain of haemoglobin. This peptide is intermediate in the course of batch hydrolysis and is rapidly degraded. Indeed, it shows an optimum at 3% degree of hydrolysis (i.e. 2 min of reaction time). The hydrolysis was carried out in a continuous membrane reactor with a space time (ratio of the flux to the reactor volume) set to 2 min (corresponding to optimum LVVh-7 production). This process allows the continuous production of a constant fraction of intermediate peptides containing LVVh-7 for 48 min.

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“…Much research has focused on the isolation of peptides derived from various protein sources. Numerous biologically active peptides have already been obtained by hydrolysis of casein [4], soya proteins [5], gluten [6], tuna myoglobin [7] and others.…”

Section: Introductionmentioning

confidence: 99%

A kinetic study of bovine haemoglobin hydrolysis by pepsin immobilized on a functionalized alumina to prepare hydrolysates containing bioactive peptides

Ticu

Vercaigne-Marko

Huma

et al. 2004

Biotech and App Biochem

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The hydrolysis kinetics of native and denatured haemoglobin, using pepsin immobilized on aluminium oxide, was studied in order to produce hydrolysates containing bioactive peptides. Pepsin was immobilized on acidic alumina and on 2-ethanolamine- O -phosphate (2-EAOP)-modified acidic alumina. Surface charge of the two supports was determined as a function of pH. Kinetic studies were performed at 23 degrees C in 0.1 M acetate buffer, pH 4.5. At this pH, the surface charge of the two supports was almost the same. The coating of alumina by 2-EAOP only introduced a two carbon spacer between alumina surface and the reaction medium. Adsorption on the two supports of haemoglobin, haem and peptides produced in the course of hydrolyses were compared. Fixation of 2-EAOP on a pepsin-alumina complex gave hydrolysis kinetics of urea-denatured haemoglobin close to that obtained with the same amount of pepsin in solution, but with comparatively less adsorption of peptides and complete adsorption of haem. Heterogeneous hydrolyses of haemoglobin with pepsin, immobilized on functionalized alumina, resulted in the presence of VV-haemorphin-4, VV-haemorphin-7 and neokyotorphin in the supernatants without haem, the presence of which makes further purification difficult.

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Photolabile ligands for opiate receptors

Cited by 14 publications

References 9 publications

Affinity Labels for Opioid Receptors

Affinity Labels for Opioid Receptors

Continuous production of a peptidic fraction containing the intermediate opioid peptide LVV‐haemorphin‐7 (LVVh‐7) by peptic hydrolysis of bovine haemoglobin in a continuous membrane reactor

A kinetic study of bovine haemoglobin hydrolysis by pepsin immobilized on a functionalized alumina to prepare hydrolysates containing bioactive peptides

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