Isolation and characterization of growth hormone from Atlantic cod (Gadus morhua).
Growth hormone was purified from cod pituitary extract by a simple two-step procedure involving gel filtration and reversed-phase high-performance liquid chromatography (rpHPLC). At each stage of purification, fractions were monitored by rpHPLC, SDS-polyacrylamide gel electrophoresis, and immunoblotting using anti-chum salmon growth hormone (GH) antiserum. The yield of purified hormone was 1.3 mg/g pituitary. Cod GH was found to exist in two monomeric forms (Mr = 20K and 22K) and dimeric forms (Mr = 40K and 42K). The two monomeric forms have a pI of 5.8, an identical amino acid composition, histidine as the N-terminal residue, and an identical lysyl endopeptidase peptide map. Staining with concanavalin A was observed on the 20K component only, but analysis for total reducing sugar did not confirm these results. Cod GH was found to be a potent stimulator of growth in juvenile rainbow trout which received intraperitoneal injections of the hormone. The partial amino acid sequence has been determined.
Rand-Weaver
M
M
Department of Biochemistry, University of Bergen, Bergen, Norway.
Walther
B T
BT
Kawauchi
H
H
D000595:Amino Acid Sequence; D000818:Animals; D003208:Concanavalin A; D005399:Fishes / Q000378:metabolism*; D013006:Growth Hormone / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism; D015151:Immunoblotting; D008969:Molecular Sequence Data
D003208:Concanavalin A; D013006:Growth Hormone