1982/01/01 by H.J. Ball, S.D. Neill, Lara Reid · 1 citation
Immunology and Microbiology · Medicine · Agricultural and Biological Sciences · Chemistry · #Microbial infections and disease research #Peptidase Inhibition and Analysis #Coccidia and coccidiosis research #Arginine #Aminopeptidase #Biochemistry #Mycoplasma #Biology #Microbiology #Enzyme #Chromogenic #Chromatography #Chemistry #Leucine #Amino acid
paper · pdf · doi:10.1128/jcm.15.1.28-34.1982
openalex publication_date 1982/01/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/06/11
The aminopeptidase activity of arginine-utilizing mycoplasmas was investigated with 20 aminoacyl beta-naphthylamide substrates. High levels of arginyl-beta-naphthylamide hydrolysis were demonstrated in 6 of 11 species when extracts of concentrated washed organisms were used. Relatively low arginine aminopeptidase activity was demonstrated with similar extracts from 22 species not utilizing arginine. The high level of arginine aminopeptidase activity could also be demonstrated with unwashed, unconcentrated samples of the same 6 species and also with Mycoplasma arthritidis. The procedure for preparing the extract of M. arthritidis appeared to remove the arginine aminopeptidase activity which was demonstrated to be present in the untreated culture. Fluorogenic and chromogenic tests were developed whereby this distinctive arginine aminopeptidase activity could be demonstrated within 4 h with the use of small volumes of broth culture (10 microliter) or single colonies, thus providing a rapid test for early characterization of some Mycoplasma species.