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Merck

Carboxypeptidase activity in human mycoplasmas.

Journal of bacteriology (1986-11-01)
K Shibata, T Watanabe
摘要

Mycoplasma salivarium produced citrulline, ammonia, and ATP from N-benzoylglycyl-L-arginine. The activity was inhibited by EDTA and was therefore concluded to be due to an arginine-specific carboxypeptidase. The activity was also found to exist in M. orale, M. buccale, M. faucium, and M. hominis.

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Sigma-Aldrich
马尿酸-Arg, carboxypeptidase substrate