Isolation of β-endorphin-related peptides from ox pituitary

Massey, D. E.; Smyth, Derek G.

doi:10.1042/bst0080751

Cited by 9 publications

(3 citation statements)

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“…(U.K.). Natural N-acetyl p-EP was purified from bovine pituitaries as described by Massey and Smyth (1980). Rabbit antiserum to porcine p-EP was raised as described by Zakarian and Smyth (1979).…”

Section: Methodsmentioning

confidence: 99%

“…Spinal cord-conditioned media were submitted directly to fractionation by gel filtration on a Sephadex G-75 column (70 x 0.7 cm) in 50% acetic acid. The elution position of p-EP and related peptides was determined using "'I-labelled bovine p-EP (Massey and Smyth, 1980). Fifty microliters of each 300 ~1 fraction was irnmunoassayed using the p-EP antiserum as described .…”

Section: Radioimmunoassay and Fractionation Of P-endorphin Immunoreacmentioning

confidence: 99%

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Evidence for the Neurotrophic Regulation of Collagen‐Tailed Acetylcholinesterase in Immature Skeletal Muscle by β‐Endorphin

Haynes

Smith

Smyth³

1984

Journal of Neurochemistry

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Acetylcholinesterase (AChE) was extracted in a high-saline medium from gastrocnemius muscles of rat embryos and young rats aged 14 days' gestation to 40 days post partum. The molecular forms of the enzyme were separated by low-salt precipitation, followed by velocity sedimentation. During gestation, all molecular forms increased in activity, particularly the 16 S (A12) form. During the first 2 weeks of life, there was a large increase in the activity of soluble AChE (G forms), whilst the activity of insoluble AChE (A forms) was reduced. Denervation of the muscle reversed the change in the relative proportions of the molecular forms. The embryonic pattern of activities of AChE forms persisted in cultures of myotubes obtained at 20 days' gestation and maintained in the absence of spinal cord. When myotubes were maintained in medium previously conditioned by developing spinal cord explants, 16 S AChE declined while the soluble (4 and 6 S) forms increased in activity in a manner resembling that seen in early postnatal muscles in vivo. beta-Endorphin (beta-EP) immunoreactivity was detected in the spinal cord-conditioned medium and was identified by HPLC and ion-exchange chromatography as beta-EP-(1-31) plus its shortened and N-acetylated forms. Cultivation of myotubes in the presence of synthetic camel beta-EP resulted in a reversible change in the pattern of AChE forms which was similar to that seen with spinal cord-conditioned medium. These studies provide evidence for the neuroregulation of AChE A and G forms in immature skeletal muscle. A major candidate for this role is beta-EP, produced and released by developing spinal cord.

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Section: Methodsmentioning

confidence: 99%

Section: Radioimmunoassay and Fractionation Of P-endorphin Immunoreacmentioning

confidence: 99%

Evidence for the Neurotrophic Regulation of Collagen‐Tailed Acetylcholinesterase in Immature Skeletal Muscle by β‐Endorphin

Haynes

Smith

Smyth³

1984

Journal of Neurochemistry

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“…Llniversity of Leeds. |I|,-Endorphin (bovine), |)p-endorphin (porcine), |)p-endorphin 1-27, |ip-endorphin 1-26 and the «.N-acetyl derivatives of the porcine peptides were isolated from bovine or porcine pituitary [6][7][8][9]. Immediately before use these peptides were purified by HPLC [10] to remove sulphoxides formed on storage.…”

Section: Methodsmentioning

confidence: 99%

Use of <sup>125</sup>I-Tyr<sup>27</sup> β-Endorphin for the Study of β-Endorphin Binding Sites in Rat Cortex

Toogood¹,

McFarthing²,

Hulme³

et al. 1986

Neuroendocrinology

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An iodine-labelled derivative of β-endorphin, ¹²⁵I-Tyr²⁷ β_h-endorphin, was used in carrier-free form to study the binding of β-endorphin to brain opioid receptors. The experiments were carried out with rat cortex membranes in vitro under conditions that gave a high degree of naloxone reversible binding. β_h-Endorphin and nonradioactive iodo-Tyr²⁷ β_h-endorphin were found to be identical in their ability to inhibit the binding of ^l25I-Tyr²⁷ β_h-endorphin. Competition experiments demonstrated the existence of binding sites with higher affinity for β-endorphin than for a variety of other opioids, including naturally occurring fragments of β-endorphin. The experiments show that ¹²⁵I-Tyr²⁷ β-endorphin possesses similar binding properties to the unmodified peptide and can be used with the advantages of iodine-¹²⁵ as an isotope for the investigation of β-endorphin receptors in brain. In experiments employing ¹²⁵I-Tyr²⁷ β-endorphin 1 -27 as the radioiodinated ligand, binding curves were obtained which showed that β-endorphin 1–31 was more potent than β-endorphin 1–27 in inhibiting the binding of the labelled 27 residue peptide. With both the 27 and 31 residue radioligands, magnesium ion enhanced the specific binding whereas sodium ion and guanylyl-imidodiphosphate had a strong inhibitory effect. The data indicate that β-endorphin 1–27 binds with reduced affinity to the same receptors as β-endorphin 1–31 and like the 31 residue peptide exhibits properties characteristic of an agonist.

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β‐Endorphin‐Related Peptides in the Pituitary Gland: Isolation, Identification and Distribution

Smyth¹,

Zakarian²,

Deakin³

et al. 1981

Novartis Foundation Symposia

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Isolation of β-endorphin-related peptides from ox pituitary

Cited by 9 publications

References 0 publications

Evidence for the Neurotrophic Regulation of Collagen‐Tailed Acetylcholinesterase in Immature Skeletal Muscle by β‐Endorphin

Evidence for the Neurotrophic Regulation of Collagen‐Tailed Acetylcholinesterase in Immature Skeletal Muscle by β‐Endorphin

Use of <sup>125</sup>I-Tyr<sup>27</sup> β-Endorphin for the Study of β-Endorphin Binding Sites in Rat Cortex

β‐Endorphin‐Related Peptides in the Pituitary Gland: Isolation, Identification and Distribution

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