Release and activation of a particulate bound acid phosphatase from Tetrahymena pyriformis

John Williams, Pei Show Juo

Research output: Contribution to journalArticle

7 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)120-126
Number of pages7
JournalBBA - Enzymology
Volume422
Issue number1
DOIs
StatePublished - Jan 23 1976
Externally publishedYes

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Tetrahymena pyriformis
Octoxynol
Acid Phosphatase
Enzymes
Membrane Lipids
Chloroform
Membrane Proteins
Proteins

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Release and activation of a particulate bound acid phosphatase from Tetrahymena pyriformis. / Williams, John; Juo, Pei Show.

In: BBA - Enzymology, Vol. 422, No. 1, 23.01.1976, p. 120-126.

Research output: Contribution to journalArticle

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