Phosphoprotein phosphatase in bovine tracheal smooth muscle Multiple fractions and multiple substrates

Elisabeth Paietta, Howard Sands

Research output: Contribution to journalArticle

8 Scopus citations

Abstract

Phosphoprotein phosphatase (phosphoprotein phosphohydrolase, EC 3.1.3.16) from bovine tracheal smooth muscle extracts was isolated and its activity determined using two [32P]phosphorylated proteins as substrates, i.e. phosphorylated histone (H-P) and a phosphorylated muscle specific substrate protein (MS-P) for the tracheal smooth muscle protein kinase. The enzyme was purified by the use of DEAE-cellulose followed by a two stage chromatography on a histone-Sepharose affinity column. Elution from the affinity column resolved the phosphoprotein phosphatase into four activity fractions. While fractions expressed phosphatase activity against both tested substrates the relative amounts of either activity varied. The ratio of activity towards H-P to activity towards MS-P changed from 11.5 to 0.12. The characterization of four phosphoprotein phosphatase fractions was based on the differences found in the following parameters: substrate specificity; sensitivity to NaF; influences of nucleotides (ATP, 5′-AMP, cyclic AMP, cyclic GMP) and the requirement of Mn2+ for maximal activity. Mg2+, Ba2+ or Ca2+ could not substitute for Mn2+.

Original languageEnglish (US)
Pages (from-to)121-132
Number of pages12
JournalBBA - Enzymology
Volume523
Issue number1
DOIs
StatePublished - Mar 14 1978
Externally publishedYes

ASJC Scopus subject areas

  • Medicine(all)

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