Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
21
pubmed:dateCreated
1982-12-18
pubmed:abstractText
Mice were immunized against chick ribosomes with the use of various protocols and immunogen preparations. Hybridomas were prepared, clones screened, and specific antibodies identified by reversible protein staining followed by immunoperoxidase staining on nitrocellulose blots. Clones were obtained which secreted specific antibodies against ribosomal proteins S6, L7, L18a, P1/P2, and also against ribosomal RNA. Antibodies were typed by means of a dot-binding assay with typing antibodies immobilized on a solid support of nitrocellulose, and also characterized by their species cross-reactivities. The common determinant on proteins P1 and P2 cross-reacted with proteins of similar molecular weight in all eucaryotes tested, and with a determinant in a previously uncharacterized 38,000-dalton protein of the large ribosomal subunit. We designate this protein P0. The determinant of P0 was also present in a protein of similar molecular weight in all eucaryotes tested. Unlike P1 and P2, P0 was not removable from ribosomes by an ethanol-NH4Cl washing procedure. No evidence for a precursor-product relationship between P0 and P1/P2 was found. P0, P1, and P2 were found in active polysomes and in the nucleolus. The molecular weights of the nucleolar forms were not identical with those of the cytoplasmic forms, suggesting some processing during ribosomal assembly and/or transport.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
257
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12709-15
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Monoclonal antibodies against eucaryotic ribosomes. Use to characterize a ribosomal protein not previously identified and antigenically related to the acidic phosphoproteins P1/P2.
pubmed:publicationType
Journal Article