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Medical Biochemistry Commons

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Dartmouth Scholarship

Viral

Medical Microbiology

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Full-Text Articles in Medical Biochemistry

The Growth Of Simian Virus 40 (Sv40) Host Range/Adenovirus Helper Function Mutants In An African Green Monkey Cell Line That Constitutively Expresses The Sv40 Agnoprotein., Terryl P. Stacy, Michele Chamberlain, Susan Carswell, Charles N. Cole Jul 1990

The Growth Of Simian Virus 40 (Sv40) Host Range/Adenovirus Helper Function Mutants In An African Green Monkey Cell Line That Constitutively Expresses The Sv40 Agnoprotein., Terryl P. Stacy, Michele Chamberlain, Susan Carswell, Charles N. Cole

Dartmouth Scholarship

The simian virus 40 T-antigen carboxy-terminal mutants, dlA2459 and dlA2475, are cell line and temperature dependent for growth and plaque formation in monkey kidney cells. Although these mutants did form plaques on BSC-1 cells at 37 degrees C, they were about fivefold less efficient for plaque formation than wild-type simian virus 40. These mutants did not grow in CV-1 cells and did not synthesize agnoprotein in those cells. CV-1 cells which constitutively express the agnoprotein were permissive for mutant plaque formation. However, late mRNAs, virion proteins, and progeny virion yields did not accumulate to wild-type levels during mutant infection of …


Proteins Antigenically Related To The Human Erythrocyte Glucose Transporter In Normal And Rous Sarcoma Virus-Transformed Chicken Embryo Fibroblasts., Donald W. Salter, Stephen A. Baldwin, Gustav E. Lienhard, Michael J. Weber Mar 1982

Proteins Antigenically Related To The Human Erythrocyte Glucose Transporter In Normal And Rous Sarcoma Virus-Transformed Chicken Embryo Fibroblasts., Donald W. Salter, Stephen A. Baldwin, Gustav E. Lienhard, Michael J. Weber

Dartmouth Scholarship

Antibody raised against the purified human erythrocyte glucose transporter specifically precipitated four proteins from normal and Rous sarcoma virus-transformed chicken embryo cells: a major protein of Mr 41,000 and minor proteins of Mr 68,000, 73,000, and 82,000. The Mr 41,000 and 82,000 proteins were found only in a membrane fraction, not in the soluble fraction, and displayed a heterogeneous mobility on NaDodSO4/polyacrylamide gel electrophoresis, suggesting glycosylation. The Mr 41,000 and 82,000 proteins were increased in amount after malignant transformation in direct proportion to the increase in hexose transport rate, and the increase was dependent on the expression of the src …