The major erythrotropin of bovine Cohn fraction V has the N-terminal sequence of insulin-like growth factor II with isoleucine at position 35.
The major erythrotropin-like factor of bovine Cohn Fraction V has been isolated from commercial albumin preparations by reversed-phase HPLC. The N-terminal sequence of the major fraction with erythrotropin-like activity is practically identical to the sequence of bovine insulin-like growth factor II. Within the first 45 amino acids, the only difference was the presence of an isoleucine instead of a serine at amino acid 35. This substitution may affect the immunoreactivity of this peptide using antibodies against bovine or human insulin-like growth factor II.
Endocrine Laboratory, Royal Victoria Hospital, Montreal, Canada.
L F
LF
Congote
F
F
Esch
D000595:Amino Acid Sequence; D000818:Animals; D001798:Blood Proteins / Q000032:analysis*; D002417:Cattle; D007335:Insulin-Like Growth Factor II / Q000235:genetics*; D036341:Intercellular Signaling Peptides and Proteins; D007532:Isoleucine; D010455:Peptides / Q000032:analysis* / Q000235:genetics; D012689:Sequence Homology, Nucleic Acid; D013002:Somatomedins / Q000235:genetics*
D001798:Blood Proteins; C043965:Cohn fraction V; D036341:Intercellular Signaling Peptides and Proteins; D010455:Peptides; D013002:Somatomedins; D007532:Isoleucine; D007335:Insulin-Like Growth Factor II; C039299:erythrotropin