Isolation of endogenous hemorphin-related hemoglobin fragments from bovine brain.
Six short-chain peptides were isolated from an acidic extract of bovine brain in the course of total peptide screening. Their primary structures determined by Edman degradation were LVVYP, LVVYPWT, LVVYPWTQ, LVVYPWTQRF, VVYPWTQ and VVYPWTQRF, which respectively corresponded to the fragments 31-35, 31-37,31- 38, 31-40, 32-38 and 32-40 of bovine hemoglobin beta-chain. All these peptides contained sequences of opioid peptides - hemorphins. For two of these peptides, viz. 32-38 and 31-40, isolated from other sources, an opioid activity was demonstrated formerly.
Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow.
A A
AA
Karelin
M M
MM
Philippova
E V
EV
Karelina
V T
VT
Ivanov
D000595:Amino Acid Sequence; D000818:Animals; D001923:Brain Chemistry; D002417:Cattle; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D006454:Hemoglobins / Q000737:chemistry*; D006801:Humans; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry* / Q000302:isolation & purification; D010446:Peptide Fragments / Q000737:chemistry* / Q000302:isolation & purification; D017386:Sequence Homology, Amino Acid; D013552:Swine
D006454:Hemoglobins; D009842:Oligopeptides; D010446:Peptide Fragments