Document Detail

Acid hydrolase activity during growth and encystment in Acanthamoeba castellanii.
MedLine Citation:
PMID:  187746     Owner:  NLM     Status:  MEDLINE    
The activity and sedimentation of acid phosphatase (APase), acid deoxyribonuclease (DNase), and acid ribonuclease (RNase) were investigated throughout growth and encystment in Acanthamoeba castellanii. The activities/mg protein of all 3 hydrolases are high in young cultures and decrease to constant levels in postlog cells. The RNase activity/ameba decreases 50% during growth, whereas the activity/cell of both APase and DNase remains constant. The percent sedimentation at 20,000 g of all 3 enzymes gradually increases from about 40% in midlog to a plateau of 80% in postlog cells. During encystment, the sedimentation behavior of RNase differs from that of APase and DNase. Encystment is characterized by a differential decrease in the activity/cell of the 3 hydrolases, with RNase decreasing most rapidly and APase least rapidly. APase is unique in that a transient increase of its specific activity is noted during encystment, even though its activity/cell is decreasing.
S M Martin; T J Byers
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The Journal of protozoology     Volume:  23     ISSN:  0022-3921     ISO Abbreviation:  J. Protozool.     Publication Date:  1976 Nov 
Date Detail:
Created Date:  1977-02-24     Completed Date:  1977-02-24     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985197R     Medline TA:  J Protozool     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  608-13     Citation Subset:  IM    
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MeSH Terms
Acid Phosphatase / metabolism
Amoeba / enzymology,  growth & development*
Deoxyribonucleases / metabolism
Phosphoric Monoester Hydrolases / metabolism*
Ribonucleases / metabolism
Reg. No./Substance:
EC 3.1.-/Deoxyribonucleases; EC 3.1.-/Ribonucleases; EC 3.1.3.-/Phosphoric Monoester Hydrolases; EC Phosphatase

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