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Evidence for Lysosomal Enzymes in Acanthamoeba and Their Activity Changes During Encystment

Please use this identifier to cite or link to this item: http://hdl.handle.net/1811/22419

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dc.creator Martin, Scott M. en_US
dc.creator Byers, Thomas J. en_US
dc.date.accessioned 2006-07-07T01:34:56Z
dc.date.available 2006-07-07T01:34:56Z
dc.date.issued 1977-01 en_US
dc.identifier.citation The Ohio Journal of Science. v77, n1 (January, 1977), 28-35 en_US
dc.identifier.issn 0030-0950 en_US
dc.identifier.uri http://hdl.handle.net/1811/22419
dc.description Author Institution: Graduate Program in Zoology and Department of Microbiology, The Ohio State University en_US
dc.description.abstract Assays on cell-free homogenates of Acanthamoeba castellanii reveal that the three hydrolases, acid phosphatase (APase), acid deoxyribonuclease, and acid ribonuclease (RNase), possess pH optima of 5.0, 4.8, and 5.2, respectively. These enzymes exhibit an enhanced sedimentation at 20,000 x g when sucrose is in the homogenizing buffer. Treatment of homogenates with Triton X-100 increases total enzyme activity. These results suggest that the enzymes are particle-bound in lysosomes. During encystment there is a differential decrease in the activity per cell of all three enzymes, with RNase decreasing most rapidly and APase least rapidly. The specific activity of APase increases during encystment even though its activity per cell gradually decreases. en_US
dc.format.extent 494594 bytes
dc.format.mimetype application/pdf
dc.language.iso en_US
dc.title Evidence for Lysosomal Enzymes in Acanthamoeba and Their Activity Changes During Encystment en_US