Partial purification of a metalloprotease catalyzing the processing of adrenodoxin precursor in bovine adrenal cortex mitochondria.

Partial purification of a metalloprotease catalyzing the processing of adrenodoxin precursor in bovine adrenal cortex mitochondria. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Partial purification of a metalloprotease catalyzing the processing of adrenodoxin precursor in bovine adrenal cortex mitochondria. Abstract Text:

Y Sagara,A Ito,T Omura,

In vitro translation of bovine adrenal cortex RNA in rabbit reticulocyte lysate cell-free system produced the precursor form of adrenodoxin having a molecular weight of approximately 22,000 daltons, which was about 10,000 daltons larger than mature adrenodoxin. The precursor of adrenodoxin was efficiently imported into adrenal cortex mitochondria in vitro. The precursor was also imported into rat liver mitochondria, suggesting the lack of tissue specificity and species specificity of the import process. The enzyme which processed the precursor of adrenodoxin to the mature form was in the matrix fraction from bovine adrenal cortex mitochondria, and the processing protease was partially purified from the matrix fraction. The apparent molecular weight of the processing protease was about 60,000 daltons as determined by Sephadex G-150 gel filtration, and its activity was optimal at pH 8.5. The processing protease was not inhibited by various bacterial protease inhibitors examined. Metal chelators (EGTA, GTP, 8-hydroxyquinoline, and Zincon) inhibited the processing, and EDTA and o-phenanthroline were more strongly inhibitory than other chelators. The processing protease was completely inactivated by incubation with 10 microM EDTA, and its activity was restored by addition of excess amounts of Mn2+, Fe2+, or Co2+. These results indicate that the maturation of the precursor of adrenodoxin is catalyzed by a soluble metalloprotease in the matrix.

Partial purification of a metalloprotease catalyzing the processing of adrenodoxin precursor in bovine adrenal cortex mitochondria. Publishing Authors By Initials

Y Sagara,A Ito,T Omura,

For similar proteins: protein precursors research abstracts see: proteins: protein precursors research

PUBMED ID PMID:

MEDLINE DATE:

Partial purification of a metalloprotease catalyzing the processing of adrenodoxin precursor in bovine adrenal cortex mitochondria. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 96

Page Numbers: 1743-52

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Dec

YEAR: 1984

Partial purification of a metalloprotease catalyzing the processing of adrenodoxin precursor in bovine adrenal cortex mitochondria. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Partial purification of a metalloprotease catalyzing the processing of adrenodoxin precursor in bovine adrenal cortex mitochondria. Keywords Mesh Terms:

KEYWORDS: Protein Precursors

MESH TERMS: metabolism

Chemical & Substance for Abstract: Partial purification of a metalloprotease catalyzing the processing of adrenodoxin precursor in bovine adrenal cortex mitochondria. Information

Substance Name: Metalloendopeptidases

Registry Number: EC 3.4.24.-

Grant and Affiliation Information for Partial purification of a metalloprotease catalyzing the processing of adrenodoxin precursor in bovine adrenal cortex mitochondria.

AFFILIATION:

Country: JAPAN

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biochem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Partial purification of a metalloprotease catalyzing the processing of adrenodoxin precursor in bovine adrenal cortex mitochondria Related Publications

• Acetanilide-hydrolyzing esterase of rat liver microsomes. I. Solubilization, purification, and intramicrosomal localization.
• Acetanilide-hydrolyzing esterase of rat liver microsomes. II. Turnover studies.
• Actinocatenispora sera sp. nov., isolated by long-term culturing.
• Actinohivin, a novel anti-HIV protein from an actinomycete that inhibits syncytium formation: isolation, characterization, and biological activities.
• Biogenesis of endoplasmic reticulum membrane in rat liver cells. I. Intracellular sites of synthesis of cytochrome b5 and NADPH-cytochrome c reductase.
• Biogenesis of endoplasmic reticulum membrane in rat liver cells. II. Discharge of the nascent peptides of NADPH-cytochrome c reductase and cytochrome b5 on the cytoplasmic side of the endoplasmic reticulum membrane.
• Biogenesis of the mitochondrial matrix enzyme, glutamate dehydrogenase, in rat liver cells. I. Subcellular localization, biosynthesis, and intracellular translocation of glutamate dehydrogenase.
• Biogenesis of the mitochondrial matrix enzyme, glutamate dehydrogenase, in rat liver cells. II. Significance of binding of glutamate dehydrogenase to microsomal membrane.
• Bone with a vascular flap induced from fat tissue with the use of rhBMP-2 in rats.
• Design and synthesis via click chemistry of 8,9-anhydroerythromycin A 6,9-hemiketal analogues with anti-MRSA and -VRE activity.
• Different turnover behavior of phenobarbital-induced and normal NADPH-cytochrome c reductases in rat liver microsomes.
• Distribution of hepatic sulfite oxidase among subcellular organelles and its intraorganelle localization.
• Inhibition of 6-methylsalicyclic acid synthesis by the antibiotic cerulenin.
• Inhibition of the biosynthesis of leucomycin, a macrolide antibiotic, by cerulenin.
• Isolation and Structure Elucidation of Seco-neokadsuranic Acid A and 3,4-Seco-(24Z)-lanosta-4(30),8,24-triene-3,26-dioic Acid1.
• Isolation and structure elucidation of 12beta-acetoxycoccinic Acid, 12beta-hydroxycoccinic Acid, 12alpha-acetoxycoccinic Acid, and 12alpha-hydroxycoccinic acid1.
• Microbacterium sediminicola sp. nov. and Microbacterium marinilacus sp. nov., isolated from marine environments.
• Potential therapeutics for obesity and atherosclerosis: inhibitors of neutral lipid metabolism from microorganisms.
• Presence of apo-cytochrome beta 5 in microsomes from rat liver.
• Prevalence of Primary Aldosteronism: Should We Screen for Primary Aldosteronism before Treating Hypertensive Patients with Medication?
• Purification and Chemical Properties of Anti-complementary Polysaccharide from the Leaves of Artemisia princeps.
• Purification and properties of NADH-cytochrome b5 reductase solubilized by lysosomes from rat liver microsomes.
• Solubilization of NADH-cytochrome b5 reductase from liver microsomes by lysosomal digestion.
• Stability of messenger RNA's for microsomal NADPH-cytochrome c reductase and cytochrome b 5 in the livers of normal and phenobarbital-treated rats.
• Structural Characterization of Anti-Complementary Polysaccharides from the Leaves of Artemisia princeps.
• Subfractionation of rat liver microsomes by immunoprecipitation and immunoadsorption methods.
• The early stage of labeling of microsomal membrane proteins in rat liver by radioactive amino acids.
• The nucleases from Acrocylindrium sp. I. Purification and properties of ribonuclease.
• Triterpenoid Acids from Kadsura longipedunculata. Neokadsuranic Acids B and C: Two Novel Triterpenoids with 14 (13 --> 12)abeo-Lanostane Skeletons.
• Yemuoside YM7, YM11, YM13, and YM14: Four Nortriterpenoid Saponins from Stauntonia chinensis.