Abstract
Transformation of hamster embryo cells by herpes simplex virus stimulated the production of a 35-kilodalton (35K) protein that was specifically immunoprecipitated, along with other polypeptides, by rabbit hyperimmune serum. This 35K polypeptide was further analyzed by partial digestion with Staphylococcus aureus V8 protease in parallel with a 35K polypeptide from herpes simplex virus type 2-infected cells. These polypeptides had almost identical partial-proteolytic cleavage maps, indicating that they are probably the same or that they are very similar polypeptides.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
