Kinetic analyses of the membrane-bound alkaline phosphatase activity of hymenolepis diminuta (cestoda: Cyclophyllidea) in relation to development of the tapeworm in the definitive host

✍ Scribed by Peter W. Pappas

• Publisher: John Wiley and Sons
• Year: 1984
• Tongue: English
• Weight: 358 KB
• Volume: 25
• Category: Article
• ISSN: 0730-2312
• DOI: 10.1002/jcb.240250303

✦ Synopsis

The specific activities of the alkaline phosphatase (APase), type I phosphodiesterase and 5'-nucleotidase activities associated with the brush-border plasma membrane of the tapeworm, Hymenolepis diminuta, decrease significantly as the tapeworm grows and matures. Kinetic analyses of the APase activity associated with membrane preparations from whole 6-, 12-, and 18-d-old H diminuta, and individual pieces of 18-d-old H diminuta cut into ten pieces of equal length, failed to demonstrate qualitative changes in the APase activity. Therefore, the decreased specific activities are apparently due to changes in the ratios of enzymatically active to enzymatically inactive membrane proteins (ie, quantitative changes in the membrane proteins) which occur as the tapeworm grows.