@article{mbs:/content/journal/micro/10.1099/13500872-140-2-417, author = "Robertson, Colin D. and Coombs, Graham H.", title = "Multiple high activity cysteine proteases of Leishmania mexicana are encoded by the Imcpb gene array", journal= "Microbiology", year = "1994", volume = "140", number = "2", pages = "417-424", doi = "https://doi.org/10.1099/13500872-140-2-417", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/13500872-140-2-417", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", keywords = "amino acid sequence", keywords = "cysteine proteases", keywords = "Imcpb genes", keywords = "Leishmania mexicana", abstract = "Summary: The interrelationship of the multiple cysteine proteases (CPs) found characteristically at high activity in Leishmania mexicana amastigotes has been investigated. The mature forms of the five enzymes of groups B and C, which have subtly different substrate preferences, are the same size. Enzymically deglycosylated group A CP proteins also have the same molecular mass. Proteases of all three groups are specifically recognized by antisera raised against the group B or group C CPs. In addition, CPs of groups A, B and C have highly similar N-terminal amino acid sequences. The consensus sequence matches that predicted from the sequenced Imcpb gene, which occurs in a tandem array of over ten similar genes. Thus, the results are consistent with the groups A, B and C CPs being products of different Imcpb genes within the array, the different genes encoding CPs with identical N-termini, but with limited amino acid substitutions within the mature enzyme accounting for the different properties of the CPs. Evidence is also presented to indicate membrane-association of proteolytically active but less processed forms of Imcpb products.", }