C-FRAGMENT OF LIPOTROPIN-AN ENDOGENOUS POTENT ANALGESIC PEPTIDE
نویسندگان
چکیده
منابع مشابه
Conformational properties of the opiate peptide C-fragment, and related peptides from lipotropin [proceedings].
found no increase in ribonuclease activity in the postmitochondrial supernatant from the muscle of alloxan-diabetic rats when we followed the conversion of 3zP-labelled rRNA into acid-soluble fragments (Table 1). It is likely therefore that the putative ribonuclease is a relatively specific endonuclease releasing large oligonucleotides which are insoluble in acid. In view of the net breakdown o...
متن کاملProteolysis of lipotropin C-fragment takes place extracellularly to form gamma-endorphin and [methionine]enkephalin [proceedings].
The octapeptide 61-68 and the heptapeptide 61-67 do not possess the protected conformation of C-fragment. In contrast with the protracted exposure to membrane enzymes required to form [methioninelenkephalin from C-fragment, the short peptides rapidly undergo this conversion. The corresponding tripeptide Thr-Ser-Glu and dipeptide Thr-Ser were isolated. The results suggest that C-fragment is degr...
متن کاملInfluence ofN-terminal acetylation and C-terminal proteolysis on the analgesic activity of ,-endorphin
Removal of one, two and four amino-acid residues from the C-terminus of f,-endorphin ('lipotropin C-Fragment', lipotropin residues 61-91) led to the formation of peptides with progressively decreased analgesic potency; there was no change in the persistence of the analgesic effects. The four C-terminal residues are thus important for the activity of f1-endorphin, but not for the duration of act...
متن کاملStructure of an Fab fragment against a C-terminal peptide of hCG at 2.0 A resolution.
3A2 is an antibody raised against human chorionic gonadotropin and recognizes a linear epitope on the C-terminal peptide of the human chorionic gonadotropin beta-subunit. Its three-dimensional structure has been determined to 2-A resolution using molecular replacement and refined to a conventional R-factor of 18.2%. The protein exhibits the typical immunoglobulin fold, and the model contains 94...
متن کاملDynorphin--still an extraordinarily potent opioid peptide.
This issue of Molecular Pharmacology is dedicated to Dr. Avram Goldstein, the journal's founding editor and one of the leaders in the development of modern pharmacology. This article focuses on his contributions to the discovery of the dynorphins and evidence that members of this family of opioid peptides are endogenous agonists for the kappa opioid receptor. In his original publication describ...
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ژورنال
عنوان ژورنال: British Journal of Pharmacology
سال: 1977
ISSN: 0007-1188
DOI: 10.1111/j.1476-5381.1977.tb07521.x