Abstract
A sedimentable form of acid phosphatase (EC 3.1.3.2) from Tetrahymena pyriformis was found to be solubilized by Triton X-100. The total enzyme activity in the insoluble cell fraction increased almost 200% upon solubilization with Triton X-100 or Nonidet P-40. Removal of membrane lipids and Triton X-100 from the particulate wash solution with a chloroform extraction resulted in non-specific enzyme protein aggregation which was reversible upon addition of Triton X-100. The results indicate that this acid phosphatase is an integral membrane protein. The pH optima for this particulate bound acid phosphatase was 3.5 with o-carboxyphenyl phosphate and 4.0 with p-nitrophenyl phosphate as substrates. The Km values of each substrate were 3.1 and 0.031 mM, respectively.
Original language | English (US) |
---|---|
Pages (from-to) | 120-126 |
Number of pages | 7 |
Journal | BBA - Enzymology |
Volume | 422 |
Issue number | 1 |
DOIs | |
State | Published - Jan 23 1976 |
Externally published | Yes |
ASJC Scopus subject areas
- General Medicine