Characterization of a mitochondrial matrix protease catalyzing the processing of adrenodoxin precursor.

Characterization of a mitochondrial matrix protease catalyzing the processing of adrenodoxin precursor. Research Abstract Details 

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Characterization of a mitochondrial matrix protease catalyzing the processing of adrenodoxin precursor. Abstract Text:

T Kumamoto,A Ito,T Omura,

Adrenodoxin (Ad) is synthesized as a larger precursor (preAd) by cytoplasmic polysomes and then transported into mitochondria concomitant with its proteolytic processing to the mature form. The protease in bovine adrenal cortex mitochondria, which converts preAd to the mature form, is a metalloprotease in the matrix (Sagara, Y., Ito, A. & Omura, T. (1984) J. Biochem. 96, 1743-1752). In this study, the protease was purified about 100-fold from the matrix fraction of bovine adrenal cortex mitochondria. The partially purified protease converted not only preAd, but also the precursors of malate dehydrogenase (MDH) and 27 kDa protein (P-27) to the corresponding mature forms. However, it was inactive toward the precursors of P-450(SCC) and of P-450(11 beta). Since isolated rat liver mitochondria can import and process preAd as efficiently as bovine adrenal cortex mitochondria, we partially purified a preAd-processing protease from rat liver mitochondria and compared its properties with those of the bovine adrenal cortex enzyme. The properties of the rat liver protease were indistinguishable from those of the bovine adrenal cortex enzyme in molecular weight determined from Sephadex G-150 gel filtration, metal requirement and ability to process preMDH and preP-27. The rat liver enzyme was also inactive toward the precursors of P-450(SCC) and P-450(11 beta). These results indicate the presence in both adrenal cortex and liver mitochondria of the same type of processing protease, which processes preAd and also the precursors of some other mitochondrial proteins.

Characterization of a mitochondrial matrix protease catalyzing the processing of adrenodoxin precursor. Publishing Authors By Initials

T Kumamoto,A Ito,T Omura,

For similar cells: blood cells: erythrocytes: reticulocytes research abstracts see: cells: blood cells: erythrocytes: reticulocytes research

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Characterization of a mitochondrial matrix protease catalyzing the processing of adrenodoxin precursor. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 100

Page Numbers: 247-54

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jul

YEAR: 1986

Characterization of a mitochondrial matrix protease catalyzing the processing of adrenodoxin precursor. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Characterization of a mitochondrial matrix protease catalyzing the processing of adrenodoxin precursor. Keywords Mesh Terms:

KEYWORDS: Reticulocytes

MESH TERMS: metabolism

Chemical & Substance for Abstract: Characterization of a mitochondrial matrix protease catalyzing the processing of adrenodoxin precursor. Information

Substance Name: Peptide Hydrolases

Registry Number: EC 3.4.-

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Country: JAPAN

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MEDLINETA: J Biochem

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