Synthesis of Factor VIII Antigen by Cultured Guinea Pig Megakaryocytes (original) (raw)
Research Article Free access | 10.1172/JCI108846
Department of Medicine, Cornell University Medical College, New York 10021
Rockefeller University, New York 10021
Find articles by Nachman, R. in:JCI |PubMed |Google Scholar
Department of Medicine, Cornell University Medical College, New York 10021
Rockefeller University, New York 10021
Find articles by Levine, R. in:JCI |PubMed |Google Scholar
Department of Medicine, Cornell University Medical College, New York 10021
Rockefeller University, New York 10021
Find articles by Jaffe, E. in:[JCI](/search/results?q=author.first%5Fname%3A%22Eric A.%22+author.last%5Fname%3A%22Jaffe%22&search%5Ftype=advanced) |PubMed |Google Scholar
Published October 1, 1977 -More info
Published October 1, 1977 -Version history
Immunoprecipitates containing guinea pig Factor VIII antigen were prepared from guinea pig plasma with a cross-reacting rabbit anti-human Factor VIII. Monospecific antisera to guinea pig Factor VIII antigen were produced in rabbits by using these washed immunoprecipitates as immunogens. The resulting antisera to guinea pig Factor VIII antigen detected Factor VIII antigen in guinea pig plasma and inhibited the von Willebrand factor activity in guinea pig plasma. This antibody also detected Factor VIII antigen in a solubilized protein mixture prepared from isolated cultured guinea pig megakaryocytes. Cultured guinea pig megakaryocytes were labeled with radio-active leucine. By radioautography, 96.2% of the radio-activity was present in megakaryocytes. The radio-active Factor VIII antigen present in the solubilized cell protein mixture was isolated by immunoprecipitation and characterized by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The results demonstrate that cultured guinea pig megakaryocytes synthesize Factor VIII antigen which contains the same polypeptide subunit (mol wt 200,000) present in guinea pig plasma Factor VIII antigen.
Images.
Click on an image below to see the page. View PDF of the complete article
- Version 1 (October 1, 1977): No description