An equine growth hormone molecular species lacking the 76-92 peptidic fragment.
A new eGH molecular species was isolated and purified by reverse phase HPLC. SDS-polyacrylamide gel electrophoresis, amino acid composition, and C- and N-terminal determinations support a primary structure identical to that described by Zakin et al. (1976), except for the lack of the 76-92 peptidic fragment and the maintaining of 30% of its biological activity.
Cascone
O
O
Institute of Chemistry and Biophysical Chemistry, UBA-CONICET Faculty of Pharmacy and Biochemistry, Buenos Aires, Argentina.
Fukushima
J G
JG
Mihajlovich
V
V
Santomé
J A
JA
Biscoglio de Jiménez Bonino
M
M
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D006128:Growth / Q000187:drug effects; D013006:Growth Hormone / Q000235:genetics* / Q000302:isolation & purification / Q000494:pharmacology; D006736:Horses / Q000235:genetics*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000235:genetics
D000596:Amino Acids; D010446:Peptide Fragments; D013006:Growth Hormone