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Results for “beta-Lipotropin”

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At least 55 records · Page 3Linked to original sources
PubMed1976

beta-endorphin is a potent analgesic agent.

beta-Endorphin, an opiate-like peptide, has potent antinociceptive properties when it is administered directly into the brain and assayed in the the tail-flick, hot-plate, and writhing tests in mice and in the wet shake test in rats. On a molar basis, beta-endorphin is 18 to 33 times more potent than morphine and its actions are blocked by the specific opiate antagonist, naloxone hydrochloride. The activity of beta-endorphin in vivo is also compared to other peptides that show opiate-like activity in assays in vitro.

Analgesics, Opioid↗
PubMed1976

Circular dichroism studies of sheep beta-lipotropic hormone.

The far ultraviolet circular dichroism spectra of sheep beta-lipotropic hormone (beta-LPH) were recorded under different conditions of pH, temperature, salt concentration, and solvent composition. Results confirm the stability of the hormone in strong basic or acidic solutions; moreover, temperatures up to 50 degrees C do not seem to affect noticeably the conformation of beta-LPH. However, increasing the NaC1 concentration or addition of dioxane in the solution brings about a conformational transition of the chain, interpreted as an increase in the helical content. The method of Yang (Chen, Y.H., Yang, J. T. & Martinez, H. M. (1972) Biochemistry 11, 4120-4131) was used to compute the proportion of helical, beta, and unordered forms of the hormone chain. The proportions are compared with those obtained from Fasman's predictive method (Chou, P. Y & Fasman, G. D. (1974) Biochemistry 13, 211-221 and Chou, P. Y. & Fasman, G. D. (1974) Biochemistry 13, 222-245) based on the known amino acid sequence of beta-LPH.

Amino Acid Sequence↗
PubMed1976

Fragmentation of porcine beta-lipotropic hormone with plasmin.

Porcine beta-lipotropic hormone was digested by plasmin and the fragments released were isolated and identified. Based on the structure and the yield of the plasmin fragments and also on the time-course of the digestion, the relative sensitivity of the theoretically susceptible bonds towards the action of plasmin was estimated. The Lys79-Asn80 bond was the most susceptible to plasmin, the Arg51-Trp52 and Arg60-Tyr61 bonds were split to a lesser extent than the Lys79-Asn80 bond, but much faster than the Lys46-Met47, Lys69-Ser70 and Lys84-Asn85 bonds of the beta-lipotropic homone structure. Further lysyl and arginyl bonds of the molecule were not attacked under our experimental conditions.

Amino Acid Sequence↗
PubMed1975

[Corticotrope and melanotrope cells in cat, fox, rat and human fetus adenohypophysis: studies with induced fluorescence, cytoimmunologic technics and lead hematoxyline].

Formaldehyde-induced fluorescence, acid-catalyzed or not, methods, and immunocytology with anti-ACTH (1-24), anti-ACTH(17-39), ANTI-BETA-LPH immunserums were applied on the same preparations of cat, fox, rat and human foetus pituitaries. The superpositions of results showed that the pars intermedia and pars distalis corticomelano-lipotrophic cells of fox and cat pituitary, those of human foetal pituitary, and the purely corticotrophics cells of the rat pars distalis contained a fluorogenic probably granular compound. Moreover, the granules of the same cell types were electively revealed on our lymphilized material by plombic hematoxylin. Only the anti-beta-LPH and/or anti-beta-MSH fixing celpls exhibited hypercyanophilic, PAS-positive and bleu alcian-positive caracteristics.

Adrenal Glands↗
PubMed1975

Multipotent lipotropic hormones. In search of a pituitary cell producing multipotent LPH.

The affinity for antiserum to the multipotent lipotropic hormone (beta-LPH) was tested by immunohistochemical staining of all known cell types in normal and certain abnormal mouse, rat, and human pituitaries. Results indicate that beta-LPH has ACTH, MSH, LH and StH(GH) immunologically cross-reacting determinants. Affinities of anti-LPH for TtH and MtH (prolactin) were not detected in normal pituitaries, but thyrotropic tumor cells reacted with anti-LPH. Absorption experiments confirm that the single polypeptide hormone of the pituitary, beta-LPH, is coded for ACTH and MSH activities. The multi-functional hormone, LPH probably is secreted by the adrenotropes. In addition to ACTH and MSH, it probably contains other antigenic and biologic determinants. Some of these may accentuate its lipotropic activities; others may be incidental. These are points calling for further correlated structural, biologic, and immunologic investigations.

Adrenocorticotropic Hormone↗