Abstract
Abstract
Extracts of mouse and rat adenohypophyses have been analyzed for a low-molecular-weight variant of growth hormone (GH) known to occur in humans, the so-called “20K”-GH (mol wt = 20,000 vs 22,000 for traditional human GH). Pituitary proteins were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunostained with an antiserum raised against murine GH. Reactive and unreactive bands in close vicinity of the major GH band were fingerprinted by a peptide-mapping technique that reveals only the tyrosine-containing peptides, but can be applied to fingerprint single protein bands within gels. We found a protein band 2000 mol wt smaller than the major murine GH in both mouse and rat pituitary glands whose fingerprint resembled that of major GH. The peptide-mapping results are consistent with the interpretation that the internal deletion of amino acid residues most likely is in the same region of the molecule as in the human 20K-GH. Unlike the human 20K-GH, however, the murine counterpart showed no cross-reactivity with an antiserum raised against 22K-GH in the test system used here.
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