Alpha-keto acid dehydrogenase complexes. 8. Comparison of dihydrolipoyl dehydrogenases from pyruvate and alpha-ketoglutarate dehydrogenase complexes of Escherichia coli.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 58 ·No. 3 ·1967-09-00 ·Pages 1126-30

Pettit FH, Reed LJ

Abstract

暂无摘要

MeSH Terms

Complement Fixation Tests Dihydrolipoamide Dehydrogenase/analysis Escherichia coli/enzymology Immunodiffusion Immunoelectrophoresis Oxidoreductases/analysis

Chemicals

Oxidoreductases Dihydrolipoamide Dehydrogenase

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Pettit F H

Reed L J

References (17)

17 references, click to expand

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Enzymatically active conformers of mitochondrial malate dehydrogenase.
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Quantitative micro-complement fixation and its use in the study of antigenic structure by specific antigen-antibody inhibition.
J Immunol. 1961 Sep;87:290-5 PMID: 13783305
alpha-Keto acid dehydrogenation complexes. I. Purification and properties of pyruvate and alpha-ketoglutarate dehydrogenation complexes of Escherichia coli.
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The relation of function and structure in lipoyl dehydrogenase.
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LIPOYL DEHYDROGENASE FROM BEEF LIVER MITOCHONDRIA.
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THE CHROMOSOMAL SITE SPECIFYING A RIBOSOMAL PROTEIN IN ESCHERICHIA COLI.
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Article Info

Journal

Proceedings of the National Academy of Sciences of the United States of America

Abbr.

Proc Natl Acad Sci U S A

ISSN

0027-8424

DOI

10.1073/pnas.58.3.1126

Published

1967-09-00

Pages

1126-30

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC335757

Subset

External Links

PubMed source DOI: 10.1073/pnas.58.3.1126 PMC Full Text View journal details

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Alpha-keto acid dehydrogenase complexes. 8. Comparison of dihydrolipoyl dehydrogenases from pyruvate and alpha-ketoglutarate dehydrogenase complexes of Escherichia coli.

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