A NOVEL ENZYME IN RAT-BRAIN CONVERTING BETA-ENDORPHIN INTO METHIONINE ENKEPHALIN - AFFINITY-CHROMATOGRAPHY AND SPECIFICITY

被引：9

作者：

KOIDA, M ^{[1
]}

AONO, J ^{[1
]}

TAKENAGA, K ^{[1
]}

YOSHIMOTO, T ^{[1
]}

KIMURA, T ^{[1
]}

SAKAKIBARA, S ^{[1
]}

机构：

[1] PROT RES FDN,INST PEPTIDE,MINOH,OSAKA 562,JAPAN

来源：

JOURNAL OF NEUROCHEMISTRY | 1979年 / 33卷 / 06期

关键词：

D O I：

10.1111/j.1471-4159.1979.tb05269.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Abstract— Methionine enkephalin (met‐enk), an endogenous opioid, commonly occurs in sequences of lipotropins (LPH) and endorphins, implying a possible biosynthetic pathway for this pentapeptide. In search of the enzyme which generates met‐enk from human β‐endorphin [LPH(61‐91), β‐end], it was found that the soluble fraction of rat brain contained such activity. The enzyme was purified by ammonium sulfate fractionation (50‐80% saturation), ion‐exchange chromatography on DEAE‐Sephadex A‐50, and affinity chromatography for which LPH(64‐67) functioned as affinity ligand and eluant. The final preparation was essentially free of other peptidases, such as kininase, met‐enk degrading and post‐proline cleaving activities. Studies on specificity revealed that the enzyme selectively cleaved the Met‐Thr bond in both LPH(64‐67) and β‐end. It is possible that this enzyme participates in the biosynthesis of met‐enk in vivo. Copyright © 1979, Wiley Blackwell. All rights reserved

引用

页码：1233 / 1237

页数：5

共 25 条

[1] ASSAY METHOD OF BRAIN ENZYME CARVING BETA-ENDORPHIN INTO METHIONINE ENKEPHALIN [J].