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Results for “beta-Lipotropin”

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At least 37 records · Page 2Linked to original sources
PubMed1978

beta-Endorphin in human cerebrospinal fluid.

beta-endorphin is a brain peptide with potent morphine-like activity structurally related to the anterior pituitary hormone beta-lipotrophin (beta-L.P.H.). We have developed a radioimmunoassay for human beta-endorphin in plasma and cerebrospinal fluid (C.S.F.). Since the antiserum also reacts with beta-L.P.H., beta-endorphin was distinguished by using a second antiserum which measures beta-L.P.H. alone. With these two immunoassay systems and gel chromatography, we found beta-endorphin in all 20 C.S.F. samples tested at a concentration always higher than, but with no other relationship to, that in plasma. beta-endorphin was found in C.S.F. of patients who had hypopituitarism and undetectable plasma-beta-endorphin, suggesting that it is synthesized in the brain rather in the pituitary.

Adult↗
PubMed1979

Acupuncture in heroin addicts; changes in Met-enkephalin and beta-endorphin in blood and cerebrospinal fluid.

In heroin addicts showing features of heroin withdrawal basal beta-endorphin levels were elevated in both blood and cerebrospinal fluid (CSF) and did not change during electroacupuncture, although this therapy suppressed the clinical features of withdrawal. Met-enkephalin levels were not elevated in blood or CSF before treatment. However, successful electroacupuncture was associated with a rise in CSF met-enkephalin levels in all patients studied, although concentrations in blood did not alter.

Acupuncture Therapy↗
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↗