A UNIQUE PROENKEPHALIN-CONVERTING ENZYME PURIFIED FROM BOVINE ADRENAL CHROMAFFIN GRANULES

被引：51

作者：

MIZUNO, K

MIYATA, A

KANGAWA, K

MATSUO, H

机构：

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1982年 / 108卷 / 03期

关键词：

D O I：

10.1016/0006-291X(82)92132-5

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：

引用

收藏

页码：1235 / 1242

页数：8

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[6] AN ABOUT 50,000-DALTON PROTEIN IN ADRENAL-MEDULLA - A COMMON PRECURSOR OF [MET]ENKEPHALIN AND [LEU]ENKEPHALIN
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[8] CHARACTERIZATION OF PRO-OPIOCORTIN-CONVERTING ACTIVITY IN PURIFIED SECRETORY GRANULES FROM RAT PITUITARY NEUROINTERMEDIATE LOBE
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[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES, 1982, 79 (01): : 108 - 112
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[10] A NEW FAMILY OF ENDOGENOUS BIG MET-ENKEPHALINS FROM BOVINE ADRENAL-MEDULLA - PURIFICATION AND STRUCTURE OF DOCOSAPEPTIDE (BAM-22P) AND EICOSAPEPTIDE (BAM-20P) WITH VERY POTENT OPIATE ACTIVITY
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