Post-translational processing, metabolic stability and catalytic efficiency of oat arginine decarboxylase expressed in Trypanosoma cruzi epimastigotes-Reference-Cited by-同舟云学术

Post-translational processing, metabolic stability and catalytic efficiency of oat arginine decarboxylase expressed in Trypanosoma cruzi epimastigotes

Published:2009-07 Issue:3 Volume:122 Page:169-176
ISSN:0014-4894
Container-title:Experimental Parasitology
language:en
Short-container-title:Experimental Parasitology

Author:

Serra María P.,Senn Alejandro M.,Algranati Israel D.

Publisher

Elsevier BV

Subject

Immunology,General Medicine,Parasitology,Infectious Diseases

Reference40 articles.

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4. Spectrophotometric and steady-state kinetic analysis of the biosynthetic arginine decarboxylase of Yersinia pestis utilizing arginine analogues as inhibitors and alternative substrates;Balbo;Biochemistry,2003

5. Mouse ornithine decarboxylase is stable in Trypanosoma brucei;Bass;Journal of Biological Chemistry,1992

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