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Biomedical subjects

T C Chang

Publications and source records attributed to T C Chang.

At least 199 records · Page 11Linked to original sources

The influence of oleic acid on cAMP accumulation of thyroid plasma membrane activated by thyrotropin.

Several thyroid hormone binding inhibitors have been described in nonthyroid illness. One of the major inhibitors, oleic acid, is present in excess amounts in sera of patients with nonthyroid illness. In this study, we demonstrated that oleic acid inhibited the cAMP accumulation of thyroid plasma membrane activated by thyrotropin at 50 mumol/l and higher concentrations. In the presence of albumin, oleic acid significantly inhibited the cAMP accumulation of plasma membrane activated by thyrotropin at 2.4 mmol/l (P less than 0.01 when the albumin concentration was 40 g/l and pH was 7.4; P less than 0.001 when the albumin concentration was 20 g/l and pH was 7.2). These findings suggest that in nonthyroid illness, especially at a low albumin concentration and low blood pH, a high oleic acid concentration may influence the thyroid function directly in addition to inhibiting the thyroid hormone binding to serum protein. Oleic acid also could inhibit 5'-guanylylimidodiphosphate- and forskolin-induced cAMP production in thyroid plasma membranes. Therefore, the inhibiting effect of oleic acid may be through the action of oleic acid on the catalytic unit of the hormone-sensitive adenylate cyclase system.

Cell Membrane↗

Traumatic nasal arterio-venous malformation: a case report.

Traumatic arterio-venous malformations of the nasal bones represent a rare but well defined clinical entity. We have described a case of a traumatic soft-tissue nasal arterio-venous malformation and commented on its investigation, pathophysiology and subsequent management. As far as we are aware this represents a hitherto unrecognised complication of nasal trauma.

Adult↗

Starch phosphorylase inhibitor from sweet potato.

A protein, starch phosphorylase inhibitor, was purified from the root of sweet potato (Ipomoea batatas [L.] Lam. cv Tainon 65). It had a molecular weight of 250,000 and could be composed of five identical subunits. The isoelectric point of the inhibitor was 4.63. It was a noncompetitive inhibitor toward the sweet potato enzyme with a K(i) value of 1.3 x 10(-6) molar when glucose-1-P was the variable substrate. Because cross-reacting materials of rabbit antiphosphorylase inhibitor of sweet potato were found in three arbitrarily selected plant materials, viz. potato tuber, spinach leaf, and rice grain, the occurrence of this protein seemed universal in higher plants. By an immunofluorescence technique, the inhibitor was located in the amyloplast and cell wall where phosphorylase was also found. This implies that they may interact in vivo, and the inhibitor may play an unknown regulatory role against the plant enzyme.

Journal Article↗