The posttranslational modification of beta-endorphin in the intermediate pituitary of the toad, Bufo marinus, includes processing at a monobasic cleavage site.
Fractionation of an acid extract of 15 B. marinus intermediate pituitaries by a combination of gel filtration chromatography and cation exchange chromatography revealed one major and five minor forms of beta-endorphin in this tissue. Based on reversed-phase HPLC and immunological properties, as well as amino acid composition and primary sequence analysis, it was deduced that the sequence of the major form of B. marinus beta-endorphin is N-acetyl-YGGFMTPE. Overall, the steady-state analyses of the minor forms of beta-endorphin indicated that the posttranslational processing of beta-endorphin in the toad intermediate pituitary includes endoproteolytic cleavage at both paired basic and monobasic cleavage sites.
Dores
R M
RM
University of Denver, Department of Biological Sciences, CO 80208.
Gieseker
K
K
Steveson
T C
TC
D000595:Amino Acid Sequence; D000818:Animals; D002024:Bufo marinus; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D010450:Endopeptidases / Q000378:metabolism*; D005260:Female; D006801:Humans; D008297:Male; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010902:Pituitary Gland / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity; D001615:beta-Endorphin / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*
D001615:beta-Endorphin; D010450:Endopeptidases