Acta Botanica Sinica Volume 39 Issue 5, Pages .
Purification and Characterization of an Extracellular Protease with Unusual Peptide Bond Specificity from Xanthomonas campestris pv. malvacearum

Huang Jing, Robert K Gholson, Carol R Roberts, Mao Da-zhang and An Jin-hua

The cotton pathogen Xanthomonas campestris pv. malvacearum produces extracellular protease activity when grown in the presence of casein-proteins (skim-milk). At least three proteases are produced with apparent molecular weights of 29 kD, 38 kD and 43 kD. Protease-1 can be inhibited by phosphoramidone, EDTA and 1,10-phenanthroline and reactivated by incubating with zinc ions, suggesting that protease-1 is a metalloprotease. It was found that protease-1 only cleaved the peptide bond of aspartic acid and cysteic acid from N-terminal side, confirming previous observations. This property could be very useful for protein sequence analysis and preparation of specific peptides from larger proteins.

Xanthomonas campestris pv. malvacearum, Extracellular protease, Cotton blight
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