Improved recovery of methionine after acid hydrolysis using mercaptoethanol.
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Biomedical subjects
Publications and source records attributed to J T Potts.
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Immunological differences between human and bovine parathyroid hormones are detected with highly purified preparations of each hormone and several antisera produced against bovine parathyroid hormone. The immunological differences found show the necessity for using a reference preparation of human hormone in assays for parathyroid hormone in human serum.
Salmon ultimobranchial calcitonin has been isolated and rendered pure, as demonstrated by several chemical criteria. Its amino acid sequence was determined by means of manual Edman degradation of the intact molecule and of several peptide subfragments. Results of automated degradation provided confirmation of the structure. The salmon molecule possesses, in common with other calcitonins, a 32-amino acid peptide chain terminating in prolinamide and containing half-cystine residues at positions 1 and 7. Although the sequence of the salmon hormone differs considerably from that of the porcine, bovine and human calcitonins, the four hormones are homologous in 9 of 32 positions. The much higher biological potency possessed by the salmon calcitonin makes it of particular interest for future structure function studies.
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Cells froma human parathyroid adenoma were infected with simian virus 40 and maintained through 13 subcultures in monolayer tissue culture. For more than 9 months, these "transformed" cells contimed to produce parathyroid hormone which was identified by radioimmunoassay and density-gradient ultra centrifugation.
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