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Purification and characterisation of an esterase from the tick Boophilus microplus
Affiliation:1. Division of Vector-Borne Diseases, Centers for Disease Control and Prevention, 3156 Rampart Road, Fort Collins, CO 80521, USA;2. Minnesota Department of Health, 625 Robert St N, St. Paul, MN 55164, USA;3. Washington County Health Department, 14949 62nd St, Stillwater, MN 55082, USA;1. Department of Environmental Sciences, The Connecticut Agricultural Experiment Station, 123 Huntington Street, New Haven, CT, 06511, United States;2. Center for Vector Biology & Zoonotic Diseases, The Connecticut Agricultural Experiment Station, 123 Huntington Street, New Haven, CT, 06511, United States;3. Department of Epidemiology of Microbial Diseases, Yale School of Public Health, 60 College Street, P.O. Box 208034, New Haven, CT, 06520-8034, United States;4. Department of Entomology, The Connecticut Agricultural Experiment Station, 123 Huntington Street, New Haven, CT, 06511, United States;5. Department of Biological Sciences, Old Dominion University, 202J Mills Godwin Bldg, Norfolk, VA, 23529, United States;1. Bacterial Diseases Branch, Division of Vector-Borne Diseases, National Center for Emerging and Zoonotic Infectious Diseases, Centers for Disease Control and Prevention, 3156 Rampart Rd., Fort Collins, CO 80521, United States;2. Rickettsial Zoonoses Branch, Division of Vector-Borne Diseases, National Center for Emerging and Zoonotic Infectious Diseases, Centers for Disease Control and Prevention, 1600 Clifton Rd., Atlanta, GA 30329-4027, United States;3. Minnesota Department of Health, 625 Robert St N, St. Paul, MN 55164, United States;1. Department of Entomology and Plant Pathology, Oklahoma State University, Stillwater, OK 74074, USA;2. Department of Natural Resource Ecology and Management, Oklahoma State University, Stillwater, OK 74078, USA
Abstract:Larvae of the tick Boophilus microplus contain an esterase which appears to be important both for the feeding of the parasite on the bovine host and as a target for a protective immunological response by the host. This enzyme was purified to homogeneity as judged by several parameters and a number of physical properties measured. It was shown that the enzyme concentration may be estimated by active site titration. Kinetic properties and substrate specificity were examined, and it was found that the enzyme behaved much like the liver esterases which have been well described in the literature.
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