title: Human pituitary growth hormone: isolation and properties of two biologically active fragments from plasmin digests.
abstract: Two biologically active fragments have been isolated from plasmic digests of human pituitary growth hormone. It was shown that these two fragments were derived from the cleavage of the Arg-Thr (positions 134-135) and the Lys-Gln (positions 140-141) bonds of the hormone: one has 134 amino acids and the other 51 amino acids, respectively. The two fragments were active in the rat tibia and pigeon crop-sac tests, as well as in complement fixation experiments.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001322:Autoanalysis; D001681:Biological Assay; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D010856:Columbidae; D003168:Complement Fixation Tests; D004589:Electrophoresis, Disc; D005341:Fibrinolysin; D013006:Growth Hormone / Q000032:analysis*; D006801:Humans; D006868:Hydrolysis; D008961:Models, Structural; D010446:Peptide Fragments / Q000032:analysis / Q000302:isolation & purification* / Q000494:pharmacology; D011388:Prolactin; D051381:Rats; D013977:Tibia / Q000187:drug effects
chemical_list: D010446:Peptide Fragments; D011388:Prolactin; D013006:Growth Hormone; D005341:Fibrinolysin