The cell attachment proteins of type 1 and type 3 reovirus are differentially susceptible to trypsin and chymotrypsin

Purified native σ1 proteins from [ 35S]methionine-labeled reovirions [serotypes 1 (Ti) and 3 (T3)] were subjected to limited trypsin and chymotrypsin digestion. It was found that T1 σ1 was resistant to both trypsin and chymotrypsin, whereas T3 σ1 (49K molecular weight) was cleaved by trypsin to yiel...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Virology (New York, N.Y.) N.Y.), 1989-05, Vol.170 (1), p.62-70
Hauptverfasser:	Yeung, Michael C., Lim, Dagwood, Duncan, Roy, Shahrabadi, Mahmoud S., William Cashdollar, L., Lee, Patrick W.K.
Format:	Artikel
Sprache:	eng
Schlagworte:	Antigens, Surface - analysis Antigens, Viral - analysis Binding Sites Biological and medical sciences Cell Adhesion Molecules Chymotrypsin - pharmacology Epitopes Fundamental and applied biological sciences. Psychology Glycophorin - metabolism In Vitro Techniques L Cells (Cell Line) Mammalian orthoreovirus 3 - analysis Microbiology Molecular Weight Morphology, structure, chemical composition, physicochemical properties Neutralization Tests Peptide Fragments - analysis Precipitin Tests Protein Binding Receptors, Virus - metabolism Reoviridae - analysis reovirus 1 sigma 1 protein Trypsin - pharmacology Viral Proteins - analysis Virology
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!