Adenosine 3′: 5′-monophosphate dependent protein kinase in the lacrymal gland

A. Takáts, A. Faragó, F. Antoni

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

The properties of cyclic AMP dependent protein kinase (ATP:protein phosphotransferase, EC 2.7.1.37) of the bovine lacrymal gland were investigated. After some purification of the cell homogenate two enzyme fractions were separated by DEAE-cellulose chromatography at pH 7.5. Both fractions were activated by cyclic AMP. The cyclic AMP concentration causing 50% of the maximal activation of each enzyme was in the range of 10-8 M, and the maximal activation was caused by about 10-6 M cyclic AMP. Comparing the phosphorylation of different histone fractions, the highest cyclic AMP activation was found in the f2b histone fraction with both enzymes.

Original languageEnglish
Pages (from-to)77-80
Number of pages4
JournalBBA - Enzymology
Volume268
Issue number1
DOIs
Publication statusPublished - Apr 7 1972

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Cyclic AMP
Adenosine
Protein Kinases
Histones
DEAE-Cellulose Chromatography
Enzyme Activation
Enzymes
Cyclic AMP-Dependent Protein Kinases
Phosphorylation

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Adenosine 3′ : 5′-monophosphate dependent protein kinase in the lacrymal gland. / Takáts, A.; Faragó, A.; Antoni, F.

In: BBA - Enzymology, Vol. 268, No. 1, 07.04.1972, p. 77-80.

Research output: Contribution to journalArticle

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