Extremely thermostable L(+)-lactate dehydrogenase fromthermotoga maritima: Cloning, characterization, and crystallization of the recombinant enzyme in its tetrameric and octameric state-Reference-Cited by-同舟云学术

Extremely thermostable L(+)-lactate dehydrogenase fromthermotoga maritima: Cloning, characterization, and crystallization of the recombinant enzyme in its tetrameric and octameric state

Published:1996-05 Issue:5 Volume:5 Page:862-873
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Ostendorp Ralf,Auerbach Günter,Jaenicke Rainer

Funder

Deutsche Forschungsgemeinschaft and the Fonds der Chemischen Industrie

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.5560050508/fullpdf

Reference62 articles.

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2. Cloning, sequencing, expression and characterization of the gene encoding the 3-phosphoglycerate kinase-triosephosphate isomerase fusionprotein fro Thermotoga maritima;Beaucamp;Prot Pept Lett,1995

3. Correlation functions as a tool for protein modeling and structure analysis;Böhm;Protein Sci,1992

4. Relevance of sequence statistics for the properties of extremophilic proteins;Böhm;Int J Pept Prot Res,1994

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