Isolation and partial chemical characterization of a 64,000-dalton glycoprotein of human cytomegalovirus.
AUTOR(ES)
Clark, B R
RESUMO
A guanidinium chloride extract of [3H]glucosamine- and [35S]methionine-labeled virions plus dense bodies of human cytomegalovirus (Towne) was separated by reverse-phase high-pressure liquid chromatography. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the eluate revealed the major peak to be a glycoprotein with a relative mass of 64,000. This glycoprotein (HCMVgp64) was characterized by amino acid analysis and a high-pressure liquid chromatographic map of its tryptic peptides.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=255455Documentos Relacionados
- Isolation and characterization of phosphonoacetic acid-resistant mutants of human cytomegalovirus.
- Isolation by high-performance liquid chromatography and partial characterization of a 57,000-dalton herpes simplex virus type 1 polypeptide.
- Antibodies to a 64,000 Mr human islet cell antigen precede the clinical onset of insulin-dependent diabetes.
- Identification and characterization of three distinct families of glycoprotein complexes in the envelopes of human cytomegalovirus.
- Identification of a neutralizing epitope on glycoprotein gp58 of human cytomegalovirus.