o-Diphenoloxidase of Mycobacterium leprae separated from infecected armadillo tissues
K Prabhakaran, E B Harris, W. F. Kirchheimer
Abstract
Open-access reader
K Prabhakaran, E B Harris, W. F. Kirchheimer
Abstract
Open-access reader
We reported earlier the occurrence of a unique o-diphenoloxidase in Mycobacterium leprae recovered from lepromatous human tissues. No other source of M. leprae fro biochemical studies was available at the time. In the present report, properties of phenoloxidase in M. leprae separated from infected armadillo tissues are presented. The results show that the o-diphenoloxidase remains unaltered in the passage of the bacilli from the human to the the animal host, indicating that the enzyme is an intrinsic characteristic of the leprosy bacteria.
OpenAlex reports 9 citations for this work. Citation counts describe recorded attention and do not establish research quality.
A contribution statement is not available in the OpenAlex record.
Method details are not available in the OpenAlex metadata.
Findings are not separately available in the OpenAlex metadata.
Limitations are not available in the OpenAlex metadata.
Application details are not available in the OpenAlex metadata.
We reported earlier the occurrence of a unique o-diphenoloxidase in Mycobacterium leprae recovered from lepromatous human tissues. No other source of M. leprae fro biochemical studies was available at the time. In the present report, properties of phenoloxidase in M. leprae separated from infected armadillo tissues are presented. The results show that the o-diphenoloxidase remains unaltered in the passage of the bacilli from the human to the the animal host, indicating that the enzyme is an intrinsic characteristic of the leprosy bacteria.
Key concepts: Armadillo, Mycobacterium leprae, Biology, Leprosy, Bacilli, Microbiology, Dasypus novemcinctus, Lepromatous leprosy