Phosphorylation of acidic ribosomal proteins from rabbit reticulocytes by a ribosome-associated casein kinase

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Resumé

Udgivelsesdato: 1977-Jul-15
OriginalsprogEngelsk
TidsskriftBBA General Subjects
Vol/bind477
Udgave nummer2
Sider (fra-til)185-189
Antal sider4
ISSN0304-4165
StatusUdgivet - 15. jul. 1977

Fingeraftryk

Ribosomal Proteins
Reticulocytes
Protein S
Rabbits
Phosphoproteins
Proteins
polyacrylamide gels

Citer dette

@article{c4b616f05a4311de839d000ea68e967b,
title = "Phosphorylation of acidic ribosomal proteins from rabbit reticulocytes by a ribosome-associated casein kinase",
abstract = "Two acidic proteins from 80-S ribosomes were isolated and purified to homogeneity. The purified acidic proteins could be phosphorylated by casein kinase using [gamma-32P]ATP and [gamma-32P]GTP as a phosphoryl donor. The proteins became phosphorylated in situ, too. Sodium dodecyl sulfate polyacrylamide gel analysis of the purified acidic proteins and 80-S particles showed identical phosphoproteins in the 16 000 dalton region.",
keywords = "Adenosine Triphosphate, Animals, Caseins, Guanosine Triphosphate, Molecular Weight, Protein Kinases, Rabbits, Reticulocytes, Ribosomal Proteins, Ribosomes",
author = "Issinger, {O G}",
year = "1977",
month = "7",
day = "15",
language = "English",
volume = "477",
pages = "185--189",
journal = "B B A - General Subjects",
issn = "0304-4165",
publisher = "Elsevier",
number = "2",

}

Phosphorylation of acidic ribosomal proteins from rabbit reticulocytes by a ribosome-associated casein kinase. / Issinger, O G.

I: BBA General Subjects, Bind 477, Nr. 2, 15.07.1977, s. 185-189.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

TY - JOUR

T1 - Phosphorylation of acidic ribosomal proteins from rabbit reticulocytes by a ribosome-associated casein kinase

AU - Issinger, O G

PY - 1977/7/15

Y1 - 1977/7/15

N2 - Two acidic proteins from 80-S ribosomes were isolated and purified to homogeneity. The purified acidic proteins could be phosphorylated by casein kinase using [gamma-32P]ATP and [gamma-32P]GTP as a phosphoryl donor. The proteins became phosphorylated in situ, too. Sodium dodecyl sulfate polyacrylamide gel analysis of the purified acidic proteins and 80-S particles showed identical phosphoproteins in the 16 000 dalton region.

AB - Two acidic proteins from 80-S ribosomes were isolated and purified to homogeneity. The purified acidic proteins could be phosphorylated by casein kinase using [gamma-32P]ATP and [gamma-32P]GTP as a phosphoryl donor. The proteins became phosphorylated in situ, too. Sodium dodecyl sulfate polyacrylamide gel analysis of the purified acidic proteins and 80-S particles showed identical phosphoproteins in the 16 000 dalton region.

KW - Adenosine Triphosphate

KW - Animals

KW - Caseins

KW - Guanosine Triphosphate

KW - Molecular Weight

KW - Protein Kinases

KW - Rabbits

KW - Reticulocytes

KW - Ribosomal Proteins

KW - Ribosomes

M3 - Journal article

VL - 477

SP - 185

EP - 189

JO - B B A - General Subjects

JF - B B A - General Subjects

SN - 0304-4165

IS - 2

ER -