Abstract
An enzymatic activity that catalyzes the conversion of glandular parathyroid hormone to a smaller-molecular-weight, biologically and immunologically active form of this hormone has been extracted from normal parathyroid and other porcine tissues. The product of the conversion has the immunologic characteristics of the hormone that occurs in peripheral serum and in tissue culture medium from parathyroid explants. The enzyme is activated by chelating agents and is inhibited by high calcium concentrations, suggesting that this enzyme may be important in the regulation of secretion or metabolism of the hormone.
MeSH Terms
Animals
Antigen-Antibody Complex/analysis
Calcium/blood,metabolism,urine
Chromatography, Gel
Edetic Acid/pharmacology
Electrophoresis, Disc
Enzyme Activation/drug effects
Hydrogen-Ion Concentration
Iodine Isotopes
Methods
Molecular Weight
Parathyroid Glands/enzymology,immunology
Parathyroid Hormone/metabolism
Peptide Hydrolases/isolation & purification,metabolism
Radioimmunoassay
Swine
Temperature
Tissue Extracts
Chemicals
Antigen-Antibody Complex
Iodine Isotopes
Parathyroid Hormone
Tissue Extracts
Edetic Acid
Peptide Hydrolases
Calcium
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Fischer J A
Oldham S B
Sizemore G W
Arnaud C D
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