ENDOPEPTIDASE-24.15 IS THE PRIMARY ENZYME THAT DEGRADES LUTEINIZING-HORMONE RELEASING HORMONE BOTH INVITRO AND INVIVO

被引：99

作者：

MOLINEAUX, CJ

LASDUN, A

MICHAUD, C

ORLOWSKI, M

机构：

来源：

JOURNAL OF NEUROCHEMISTRY | 1988年 / 51卷 / 02期

关键词：

D O I：

10.1111/j.1471-4159.1988.tb01084.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：

引用

页码：624 / 633

页数：10

共 34 条

[1] SYNAPTOSOMAL MEMBRANE-BOUND FORM OF ENDOPEPTIDASE-24.15 GENERATES LEU-ENKEPHALIN FROM DYNORPHIN1-8, ALPHA-NEUENDORPHIN-BETA-NEOENDORPHIN, AND MET-ENKEPHALIN FROM MET-ENKEPHALIN-ARG6-GLY7-LEU8 [J].

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[2] LUTEINIZING-HORMONE-RELEASING HORMONE PEPTIDASE ACTIVITIES IN DISCRETE HYPOTHALAMIC REGIONS AND ANTERIOR-PITUITARY OF THE RAT - APPARENT REGULATION DURING THE PREPUBERTAL PERIOD AND 1ST ESTROUS-CYCLE AT PUBERTY [J].

ADVIS, JP ;

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[4] EVIDENCE THAT ENDOPEPTIDASE-CATALYZED LUTEINIZING-HORMONE RELEASING HORMONE CLEAVAGE CONTRIBUTES TO THE REGULATION OF MEDIAN-EMINENCE LHRH LEVELS DURING POSITIVE STEROID FEEDBACK [J].

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[5] MEMBRANE-BOUND KIDNEY NEUTRAL METALLOENDOPEPTIDASE - INTERACTION WITH SYNTHETIC SUBSTRATES, NATURAL PEPTIDES, AND INHIBITORS [J].

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ORLOWSKI, M .

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[6] MEMBRANE-BOUND PITUITARY METALLOENDOPEPTIDASE - APPARENT IDENTITY TO ENKEPHALINASE [J].

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[7]

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[8] ACTIVE-SITE DIRECTED N-CARBOXYMETHYL PEPTIDE INHIBITORS OF A SOLUBLE METALLOENDOPEPTIDASE FROM RAT-BRAIN [J].

CHU, TG ;

ORLOWSKI, M .

BIOCHEMISTRY, 1984, 23 (16) :3598-3603

[9] SOLUBLE METALLOENDOPEPTIDASE FROM RAT-BRAIN - ACTION ON ENKEPHALIN-CONTAINING PEPTIDES AND OTHER BIOACTIVE PEPTIDES [J].

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ORLOWSKI, M .

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[10]

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