tRNATrp (bovine) binding to the reverse transcriptase of avian myeloblastosis virus and function as a heterologous primer.

Abstract
The primary structures for bovine tRNATrp and primer avian tRNATrp show only minor differences in nucleotide sequence. The heterologous bovine tRNATrp appears to have properties similar to the avian tRNATrp in its ability to bind the .alpha..beta. form of RNA-dependent DNA nucleotidyltransferase of avian myeloblastosis virus. A stable enzyme-tRNA complex was isolated by gel filtration. Bovine tRNATrp can hybridize to the avian viral 35S RNA and act as a primer for transcription of the RNA. Bovine tRNATrp can be obtained in larger amounts than the avian primer and can be used to study the interactions between the primer and the viral enzyme.