Abstract

Two distinct gonadotropins, GTH I and GTH II, isolated from female chum salmon pituitary glands, were separated into subunits by acid treatment and subsequent fractionation on reversed-phase high-performance liquid chromatography. GTH II was completely dissociated in 0.1% trifluoroacetic acid, while GTH I was partially dissociated. The acidstable form of GTH I exhibited a potency identical to that of GTH I in stimulating estradiol-17β production in vitro. Both GTH I and GTH II consist of two dissimilar subunits. One subunit (α) is common to both GTHs, has Tyr as its N-terminal residue, and a molecular weight ( M r) of 22K by sodium dodecyl sulfate-polyacrylamide gel electrophoresis after reduction. The other subunit (β) has a M r of 17K and an N-terminal residue of Gly for GTH I, whereas GTH II β is 18K and has an N-terminal residue of Set, after reduction.

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