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Biomedical subjects

T C Chang

Publications and source records attributed to T C Chang.

At least 217 records · Page 12Linked to original sources
PubMed1984

Essential tyrosyl residues of human placental alkaline phosphatase.

Human placental alkaline phosphatase was inactivated with tetranitromethane in a biphasic process. Spectral and amino acid analysis demonstrated that the inactivation was due to the conversion of tyrosine residues to 3-nitrotyrosine. The inactivation process showed saturation kinetics. Protection of the enzyme against tetranitromethane inactivation was afforded by inorganic phosphate. The binding affinity between the modified enzyme and inorganic phosphate was decreased. Our results suggest the involvement of tyrosyl residues in the locus of phosphoryl site of the phosphorylated enzyme forms.

Alkaline Phosphatase↗
PubMed1983

The changes of serum titers of thyroid antibodies in patients of Graves' disease with hyperthyroidism after treatments with antithyroid drugs.

In order to investigate the effect of antithyroid drugs on serum titers of antithyroglobulin and anti-thyroid microsomal antibody, these two antibody levels were studied in 38 patients of Graves' disease with hyperthyroidism before and after treatments with carbimazole or methimazole. The results showed no consistent changes in their titers. To explain the inconsistent findings as compared with other authors' studies, lower doses of antithyroid drugs were postulated as one of the causes.

Adolescent↗
PubMed1982

Involvement of lysine residue in the nucleotide binding of pigeon liver malic enzyme: modification with affinity label periodate-oxidized NADP.

1. Periodate-oxidized NADP, a competitive inhibitor of malic enzyme with respect to NADP, inactivate the enzyme in mild conditions. 2. The inactivation is due to the modification of an essential lysine residue. 3. Two molecules of reagent were found to be incorporated into the enzyme tetramer after extensive modification. 4. Complete protection of malic enzyme from the oxidized NADP inactivation was afforded by NADP and its analogues. 5. The modified enzyme showed increased apparent Michaelis constant for the nucleotide coenzymes but the maximum velocity was decreased. 6. The binding between the modified enzyme and NADPH was impaired.

Adenosine Diphosphate↗