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J T Potts

Publications and source records attributed to J T Potts.

At least 271 records · Page 15Linked to original sources
PubMed1972

An evaluation of antibodies and clinical resistance to salmon calcitonin.

21 patients with Paget's disease of bone and one with osteoporosis were studied to detect development of antibodies to salmon calcitonin during chronic therapy. Antibody titers ranged from 1:40 to 1:30,000 in plasma obtained after treatment of 11 patients. Radio-immunoelectrophoresis revealed that the antibodies were restricted to the gammaG class. One patient, W. O., with Paget's disease initially responded to treatment with a decrease in bone turnover, but later became resistant to the hormone in association with the appearance of a very high titer (1:30,000) of antibody against salmon calcitonin. A 1:10 dilution of his plasma was shown to completely inactivate 20 mMRC units/ml of salmon calcitonin as detected by bioassay in rats; slight inactivation was detected at a 1:200 dilution. All other patients continued to respond to salmon calcitonin despite the development of antibody to the hormone in ten cases. No evidence of systemic allergic reactions or other toxicity was found in any patient. The data suggest that although antibody formation may occur in as many as 50% of patients treated with salmon calcitonin, this antibody response is unlikely to be of clinical significance in most patients. However, in an occasional patient, a marked antibody response may occur which interferes with the therapeutic use of the hormone.

Adult↗
PubMed1972

Parathyroid Hormone in Human Plasma: IMMUNOCHEMICAL CHARACTERIZATION AND BIOLOGICAL IMPLICATIONS.

Antigenic recognition of four anti-bovine parathyroid hormone antisera was characterized by their reactivity with bovine hormonal fragments (1-34, 1-13, 14-34, 19-34, 53-84) and human hormone extracted from parathyroid adenomas. All antisera were found to have antibody populations which recognized more than one antigenic determinant and all antisera differed in their specificity and reactivity for the fragments of bovine hormone. By modification of two antisera, GP-1 and GP-133, by preincubation with excess concentrations of 1-34 or 53-84 fragments, antigenic recognition was restricted to defined regions of the hormonal sequence.When assays using these modified antisera were applied to the study of hormones extracted from glands, greater immunochemical similarities were seen between bovine and human parathyroid hormone using assays that were specific for the measurement of amino-terminal portions of the hormones than of the carboxy-terminal portions.When assays using these antisera were applied to the study of endogenous parathyroid hormone in human plasma, the immunoreactive hormone in the general circulation was shown to substantially lack an amino-terminal portion of the sequence of the intact hormone, including an antigenic determinant requiring all or some of the 14-19 region. This deletion accounts, at least in part, for the immunochemical heterogeneity of plasma parathyroid hormone in man. Radioimmunoassay of fractions of peripheral plasma subjected to gel filtration confirms that the dominant form of the immunoreactive hormone in the general circulation of man is a hormonal fragment that is totally devoid of amino-terminal reactivity. Because of this deletion, it can be concluded that most of the immunoreactive parathyroid hormone in the general circulation of man must be biologically inactive.

Journal Article↗
PubMed1971

Calcitonin.

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Amino Acid Sequence↗
PubMed1971

Synthesis of a biologically active N-terminal tetratriacontapeptide of parathyroid hormone.

Determination of the amino acid sequence of bovine parathyroid hormone has led to the synthesis of a tetratriacontapeptide corresponding to the amino-terminal 1-34 residues of the native molecule. The specific biological effects of this synthetic peptide on bone and kidney are qualitatively identical to those of the native hormone in classical bioassays in vivo and in several systems in vitro. Potency of the synthetic peptide equals or exceeds that of a biologically active fragment of comparable size isolated from the native hormone; the synthetic and natural peptides show complete immunological cross-reactivity. Thus, essential requirements for the physiological actions of the peptide on both skeletal and renal tissue are contained within the 34 amino-terminal amino acids. The potency of the synthetic peptide, relative to that of the native (84-amino acid) polypeptide, is greater in vitro than in vivo; this suggests that the carboxyl terminal two-thirds of the native hormone may protect the circulating polypeptide from rapid metabolic degradation.

Adenylyl Cyclases↗