Peptides with Morphine-like Action in the Brain

1977 ◽  
Vol 130 (3) ◽  
pp. 298-304 ◽  
Author(s):  
Hans W. Kosterlitz ◽  
John Hughes

SummaryThe reasons which led to the search in the brain for substances with morphine-like actions are discussed. Two pentapeptides, methionine-enkephalin and leucine-enkephalin, were isolated. The amino acid sequence of methionine-enkephalin occurs also in the pituitary prohormone β-lipotropin, of which longer fragments (endorphins) of up to 31 amino acids exhibit strong morphine-like action.The physiological significance of these short and long opioid peptides is discussed, particularly with regard to their possible roles as neurotransmitter or neuromodulator.With regard to the mechanisms involved in the development of tolerance to and dependence on opiates, the importance of interaction between the endogenous opioid peptides and the exogenous opiate alkaloids is stressed.The possible therapeutic implications are discussed briefly.

1982 ◽  
Vol 1 (4) ◽  
pp. 195-198
Author(s):  
B. J. Meyer

In 1964 β-lipotropin, a compound consisting of 91 amino acids, was isolated from the adenohypophysis. In 1973, opiate receptors were found to be present in different areas of the brain and it was postulated that the brain probably produces opiate-like substances which react with these receptors. This finding was followed with an intensive search for opiate-like substances, resulting in the isolation of two groups of substances which react with the opiate receptors. These were named the encephalins and the endorphins. All members of these two groups were either peptides or polypeptides and the amino-acid sequence of each corresponded to the amino-acid sequence of specific segments of β-lipotropin.


1979 ◽  
Vol 42 (05) ◽  
pp. 1652-1660 ◽  
Author(s):  
Francis J Morgan ◽  
Geoffrey S Begg ◽  
Colin N Chesterman

SummaryThe amino acid sequence of the subunit of human platelet factor 4 has been determined. Human platelet factor 4 consists of identical subunits containing 70 amino acids, each with a molecular weight of 7,756. The molecule contains no methionine, phenylalanine or tryptophan. The proposed amino acid sequence of PF4 is: Glu-Ala-Glu-Glu-Asp-Gly-Asp-Leu-Gln-Cys-Leu-Cys-Val-Lys-Thr-Thr-Ser- Gln-Val-Arg-Pro-Arg-His-Ile-Thr-Ser-Leu-Glu-Val-Ile-Lys-Ala-Gly-Pro-His-Cys-Pro-Thr-Ala-Gin- Leu-Ile-Ala-Thr-Leu-Lys-Asn-Gly-Arg-Lys-Ile-Cys-Leu-Asp-Leu-Gln-Ala-Pro-Leu-Tyr-Lys-Lys- Ile-Ile-Lys-Lys-Leu-Leu-Glu-Ser. From consideration of the homology with p-thromboglobulin, disulphide bonds between residues 10 and 36 and between residues 12 and 52 can be inferred.


1964 ◽  
Vol 42 (6) ◽  
pp. 755-762 ◽  
Author(s):  
David B. Smith

An outline of present ideas concerning the arrangement, folding, and chemistry of the polypeptide chains of hemoglobin is given with some references to present know ledge of myoglobin.New material includes a partial amino acid sequence of the β-chain of horse hemoglobin, details concerning the amino acids lining the heme pocket of horse hemoglobin, and the effects of carboxypeptidases A and B on horse oxy- and horse deoxy-hemoglobin. The kinetics of the latter reactions are not simple. The C-terminal amino acids are released more rapidly from the oxygenated form.


1987 ◽  
Vol 72 (s16) ◽  
pp. 90P-91P
Author(s):  
J.R. Thornton ◽  
M.S. Losowsky

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