Lactae dehydrogenase from an extremely thermophilic Bacillus.

Archiv fur Mikrobiologie ·Vol. 85 ·No. 2 ·1972-00-00 ·Pages 113-22

Weerkamp A, Mac Elroy RD

Abstract

暂无摘要

MeSH Terms

Adenosine Diphosphate Bacillus/enzymology Chloromercuribenzoates Chromatography, Gel Culture Media Hot Temperature Hydrogen-Ion Concentration L-Lactate Dehydrogenase/analysis,isolation & purification Molecular Weight NAD Phosphoenolpyruvate Pyruvates

Chemicals

Chloromercuribenzoates Culture Media Pyruvates NAD Adenosine Diphosphate Phosphoenolpyruvate L-Lactate Dehydrogenase

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Weerkamp A

Mac Elroy R D

References (13)

13 references, click to expand

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Thermus aquaticus gen. n. and sp. n., a nonsporulating extreme thermophile.
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Characteristics and properties of a caldo-active bacterium producing extracellular enzymes and two related strains.
Arch Mikrobiol. 1972;82(1):1-23 PMID: 5025356
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Allosteric regulation of enzyme activity.
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Kinetics of Escherichia coli B D-lactate dehydrogenase and evidence for pyruvate-controlled change in conformation.
J Biol Chem. 1968 May 25;243(10 ):2587-96 PMID: 4297266
Growth conditions and temperature-dependent substrate specificity of two extremely thermophilic bacteria.
Arch Mikrobiol. 1971;76(1):2-17 PMID: 5548291
Physiology of growth at high temperatures.
J Appl Bacteriol. 1968 Mar;31(1):24-35 PMID: 4870168
The thermostable allosteric nature of fructose 1,6-diphosphatase from an extreme thermophile.
Biochem Biophys Res Commun. 1971 Oct 15;45(2):495-500 PMID: 4334342
Thermal properties of fructose-I,6-diphosphate aldolase from thermophilic bacteria.
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Article Info

Journal

Archiv fur Mikrobiologie

Abbr.

Arch Mikrobiol

ISSN

0003-9276

DOI

10.1007/BF00409292

Published

1972-00-00

Pages

113-22

Language

English

Region

Germany

NLM ID

0411220

Subset

External Links

PubMed source DOI: 10.1007/BF00409292

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Lactae dehydrogenase from an extremely thermophilic Bacillus.

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