Differences in protein phosphorylation in vivo and in vitro between wild type and dunce mutant strains of Drosophila melanogaster

Piroska Dévay, Magda Solti, I. Kiss, V. Dombrádi, P. Friedrich

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

1. 1. The protein phosphorylation patterns of wild type and dunce mutant strains of Drosophila melanogaster, as detected by sodium dodecylsulfate-gel electrophoresis and autoradiography, have been compared. 2. 2. After labelling in vivo with 32Pi or in vitro in homogenates with [γ-32P]ATP, radioactive bands at and above apparent polypeptide mol. wt ~ 110,000 were more pronounced in dunce fly heads than in wild type heads. 3. 3. When labelling in vitro, in dunceM11 there appeared a radioactive band at apparent mol. wt ≈ 53,000 that was faintly visible in the wild strain. 4. 4. The same band could be intensified in both strains by adding cyclic AMP to the homogenate or by performing homogenization in the presence of theophylline. 5. 5. The data suggest that the mol. wt % 53,000 protein is a substrate for cyclic AMP-dependent protein kinase.

Original languageEnglish
Pages (from-to)1401-1408
Number of pages8
JournalInternational Journal of Biochemistry
Volume16
Issue number12
DOIs
Publication statusPublished - 1984

Fingerprint

Phosphorylation
Drosophila melanogaster
Labeling
Head
Theophylline
Cyclic AMP-Dependent Protein Kinases
Electrophoresis
Autoradiography
Diptera
Cyclic AMP
Proteins
Adenosine Triphosphate
Gels
Sodium
Peptides
Substrates
In Vitro Techniques

ASJC Scopus subject areas

  • Biochemistry

Cite this

@article{fc80dcbbfa9549b5824b36a839d89437,
title = "Differences in protein phosphorylation in vivo and in vitro between wild type and dunce mutant strains of Drosophila melanogaster",
abstract = "1. 1. The protein phosphorylation patterns of wild type and dunce mutant strains of Drosophila melanogaster, as detected by sodium dodecylsulfate-gel electrophoresis and autoradiography, have been compared. 2. 2. After labelling in vivo with 32Pi or in vitro in homogenates with [γ-32P]ATP, radioactive bands at and above apparent polypeptide mol. wt ~ 110,000 were more pronounced in dunce fly heads than in wild type heads. 3. 3. When labelling in vitro, in dunceM11 there appeared a radioactive band at apparent mol. wt ≈ 53,000 that was faintly visible in the wild strain. 4. 4. The same band could be intensified in both strains by adding cyclic AMP to the homogenate or by performing homogenization in the presence of theophylline. 5. 5. The data suggest that the mol. wt {\%} 53,000 protein is a substrate for cyclic AMP-dependent protein kinase.",
author = "Piroska D{\'e}vay and Magda Solti and I. Kiss and V. Dombr{\'a}di and P. Friedrich",
year = "1984",
doi = "10.1016/0020-711X(84)90248-9",
language = "English",
volume = "16",
pages = "1401--1408",
journal = "International Journal of Biochemistry and Cell Biology",
issn = "1357-2725",
publisher = "Elsevier Limited",
number = "12",

}

TY - JOUR

T1 - Differences in protein phosphorylation in vivo and in vitro between wild type and dunce mutant strains of Drosophila melanogaster

AU - Dévay, Piroska

AU - Solti, Magda

AU - Kiss, I.

AU - Dombrádi, V.

AU - Friedrich, P.

PY - 1984

Y1 - 1984

N2 - 1. 1. The protein phosphorylation patterns of wild type and dunce mutant strains of Drosophila melanogaster, as detected by sodium dodecylsulfate-gel electrophoresis and autoradiography, have been compared. 2. 2. After labelling in vivo with 32Pi or in vitro in homogenates with [γ-32P]ATP, radioactive bands at and above apparent polypeptide mol. wt ~ 110,000 were more pronounced in dunce fly heads than in wild type heads. 3. 3. When labelling in vitro, in dunceM11 there appeared a radioactive band at apparent mol. wt ≈ 53,000 that was faintly visible in the wild strain. 4. 4. The same band could be intensified in both strains by adding cyclic AMP to the homogenate or by performing homogenization in the presence of theophylline. 5. 5. The data suggest that the mol. wt % 53,000 protein is a substrate for cyclic AMP-dependent protein kinase.

AB - 1. 1. The protein phosphorylation patterns of wild type and dunce mutant strains of Drosophila melanogaster, as detected by sodium dodecylsulfate-gel electrophoresis and autoradiography, have been compared. 2. 2. After labelling in vivo with 32Pi or in vitro in homogenates with [γ-32P]ATP, radioactive bands at and above apparent polypeptide mol. wt ~ 110,000 were more pronounced in dunce fly heads than in wild type heads. 3. 3. When labelling in vitro, in dunceM11 there appeared a radioactive band at apparent mol. wt ≈ 53,000 that was faintly visible in the wild strain. 4. 4. The same band could be intensified in both strains by adding cyclic AMP to the homogenate or by performing homogenization in the presence of theophylline. 5. 5. The data suggest that the mol. wt % 53,000 protein is a substrate for cyclic AMP-dependent protein kinase.

UR - http://www.scopus.com/inward/record.url?scp=0021665811&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021665811&partnerID=8YFLogxK

U2 - 10.1016/0020-711X(84)90248-9

DO - 10.1016/0020-711X(84)90248-9

M3 - Article

C2 - 6442236

AN - SCOPUS:0021665811

VL - 16

SP - 1401

EP - 1408

JO - International Journal of Biochemistry and Cell Biology

JF - International Journal of Biochemistry and Cell Biology

SN - 1357-2725

IS - 12

ER -