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Adrenal Opioid Proteins of 8600 and 12,600 Daltons: Intermediates in Proenkephalin Processing

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Specialty Science
Date 1982 Mar 1
PMID 6952256
Citations 3
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Abstract

[Met]Enkephalin-containing proteins of 8600 and 12,600 daltons have been isolated from acid extracts of bovine adrenal medulla and purified to homogeneity, and their sequences have been determined by a combination of automated Edman degradation, tryptic mapping, and enzymatic time-course hydrolysis. The 8600-dalton protein contains one copy of the [Met]enkephalin sequence at the COOH terminus and the 12,600-dalton protein contains three copies of [Met]enkephalin, of which two are internal and the third is at the COOH terminus. They possess identical NH2-terminal amino acid sequences, suggesting that the 8600-dalton protein is derived from the 12,600-dalton protein by intracellular proteolytic processing. This is supported by results from tryptic maps of both proteins. Furthermore, chemical analysis of the tryptic peptides obtained from the 12,600-dalton protein indicates that it also contains the amino acid sequence that corresponds to a previously characterized enkephalin-containing polypeptide of 3800 daltons (peptide F) [Jones et al. (1980) Arch. Biochem. Biophys. 204, 392-395]. All three polypeptides appear to be intermediates in posttranslational processing of a still larger polyenkephalin precursor molecule, proenkephalin, and part of a biosynthetic pathway leading to smaller enkephalin-containing polypeptides and free enkephalins.

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References
1.
Stein S, Bohlen P, Stone J, Dairman W, UDENFRIEND S . Amino acid analysis with fluorescamine at the picomole level. Arch Biochem Biophys. 1973; 155(1):202-12. DOI: 10.1016/s0003-9861(73)80022-0. View

2.
Wittmann-Liebold B . Amino acid sequence studies on ten ribosomal proteins of Escherichia coli with an improved sequenator equipped with an automatic conversion device. Hoppe Seylers Z Physiol Chem. 1973; 354(10-11):1415-31. DOI: 10.1515/bchm2.1973.354.2.1415. View

3.
Bohlen P, Stein S, Stone J, UDENFRIEND S . Automatic Monitoring of primary amines in preparative column effluents with fluorescamine. Anal Biochem. 1975; 67(2):438-45. DOI: 10.1016/0003-2697(75)90316-4. View

4.
Zimmerman C, Appella E, Pisano J . Advances in the analysis of amino acid phenylthiohydantoins by high performance liquid chromatography. Anal Biochem. 1976; 75(1):77-85. DOI: 10.1016/0003-2697(76)90057-9. View

5.
Gerber L, Stein S, Rubinstein M, Wideman J, UDENFRIEND S . Binding assay for opioid peptides with neuroblastoma x glioma hybrid cells: specificity of the receptor site. Brain Res. 1978; 151(1):117-26. DOI: 10.1016/0006-8993(78)90954-x. View