One-step isolation of microbial ribulose-1,5-diphosphate carboxylase.

Archives of microbiology ·Vol. 99 ·No. 3 ·1974-00-00 ·Pages 231-40

Tabita FR, McFadden BA

Abstract

暂无摘要

MeSH Terms

Carboxy-Lyases/isolation & purification Centrifugation, Density Gradient Chromatiaceae/enzymology Chromatium/enzymology Cyanobacteria/enzymology Electrophoresis, Polyacrylamide Gel Euglena gracilis/enzymology Pentoses Pseudomonas/enzymology Sucrose

Chemicals

Pentoses Sucrose Carboxy-Lyases

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Tabita F R

McFadden B A

References (24)

24 references, click to expand

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Purification and purine nucleotide regulation of ribulose-1,5-diphosphate carboxylase from Thiobacillus novellus.
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Ribulose 1,5-diphosphate carboxylase from Hydrogenomonas eutropha and Hydrogenomonas facilis. I. Purification, metallic ion requirements, inhibition, and kinetic constants.
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The isolation and preliminary characterization of a halophilic photosynthetic bacterium.
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A simple method for the isolation of fraction I protein of chloroplasts.
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A one-step method for the isolation and determination of leaf ribulose-1,5-diphosphate carboxylase.
Anal Biochem. 1971 May;41(1):57-66 PMID: 5578554
Studies on fraction-I protein. I. Effect of crystallization of fraction-I protein from tobacco leaves on ribulose diphosphate carboxylase activity.
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Article Info

Journal

Archives of microbiology

Abbr.

Arch Microbiol

ISSN

0302-8933

DOI

10.1007/BF00696237

Published

1974-00-00

Pages

231-40

Language

English

Region

Germany

NLM ID

0410427

Subset

External Links

PubMed source DOI: 10.1007/BF00696237 View journal details

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One-step isolation of microbial ribulose-1,5-diphosphate carboxylase.

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