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β protein C is not glycosylated at asparagine 329. The rate of translation may influence the frequency of usage at asparagine-X-cysteine sites

Author
MILETICH, J. P; BROZE, G. J
Washington univ. school medicine, dep. medicine, div. lab. medicine, Saint Louis MO 63110, United States
Source

The Journal of biological chemistry (Print). 1990, Vol 265, Num 19, pp 11397-11404, 8 p ; ref : 23 ref

CODEN
JBCHA3
ISSN
0021-9258
Scientific domain
Biochemistry, molecular biology, biophysics; Biotechnology
Publisher
American Society for Biochemistry and Molecular Biology, Bethesda, MD
Publication country
United States
Document type
Article
Language
English
Keyword (fr)
Cystéine Electrophorèse gel Glycoprotéine Glycosylation Homme Liaison disulfure Méthode immunoblotting Protéine C Lignée HepG2
Keyword (en)
Cysteine Gel electrophoresis Glycoproteins Glycosylation Human Disulfide bond Immunoblotting assay Protein C
Keyword (es)
Cisteina Electroforesis gel Glicoproteina Glicosilación Hombre Enlace disulfuro Proteína C
Classification
Pascal
002 Biological and medical sciences / 002A Fundamental and applied biological sciences. Psychology / 002A02 Analytical, structural and metabolic biochemistry / 002A02D Proteins / 002A02D06 Glycoproteins

Discipline
Analytical, structural and metabolic biochemistry
Origin
Inist-CNRS
Database
PASCAL
INIST identifier
19738015

Sauf mention contraire ci-dessus, le contenu de cette notice bibliographique peut être utilisé dans le cadre d’une licence CC BY 4.0 Inist-CNRS / Unless otherwise stated above, the content of this bibliographic record may be used under a CC BY 4.0 licence by Inist-CNRS / A menos que se haya señalado antes, el contenido de este registro bibliográfico puede ser utilizado al amparo de una licencia CC BY 4.0 Inist-CNRS

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