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H Stelmach

Publications and source records attributed to H Stelmach.

7 recordsLinked to original sources
PubMed1985

Activity of 5'-nucleotidase, AMP deaminase, adenosine deaminase, acid and alkaline phosphatase and nucleotide pyrophosphatase in human thyroid.

The activity of 5'-nucleotidase, AMP deaminase, adenosine deaminase, acid phosphatase, alkaline phosphatase and nucleotide pyrophosphatase was assayed in human thyroid glands. The 5'-nucleotidase activity was higher than that of AMP deaminase which suggested that AMP undergoes degradation primarily as a result of dephosphorylation in thyroid tissue. A high acid phosphatase activity was noted as compared to that of alkaline phosphatase activity. In toxic goitre the increase in adenosine deaminase and acid phosphatase was observed together with the decrease in pyrophosphatase activity.

5'-Nucleotidase↗
PubMed1984

Intracellular distribution of AMP deaminase in the pig thyroid gland.

AMP deaminase and adenosine deaminase activities were assayed in the subcellular fractions of pig thyroid gland. AMP deaminase is localized in the cytosolic fraction; however, this enzyme showed remarkable tendency to bind with the subcellular particulate fractions. Adenosine deaminase is also localized in the cytosolic fraction but in contradistinction to AMP deaminase, adenosine deaminase under the same experimental conditions has no tendency of binding to subcellular particulate fractions. The significance of AMP deaminase binding to subcellular particulate fractions is discussed.

AMP Deaminase↗
PubMed1981

Effect of iodide on glucose, N-acetylglucosamine and leucine incorporation into acid-insoluble fraction of pig thyroid proteins in vitro.

The effect of KI on D-[1-14C]glucose and N-acetyl-D-[1-14C]glucosamine incorporation into thyroid proteins was studied in vitro. It was found that KI in a concentration of 0.1 mmol 1-1 had no effect on the incorporation of the sugars under study. However, under the same experimental conditions KI inhibited L-[1-14C]leucine incorporation into proteins. It is suggested that KI, appropriate concentrations, inhibits the synthesis of peptide chains but has no effect on the incorporation of sugars into proteins.

Acetylglucosamine↗
PubMedDate not supplied

[Thyroid gland inositol-1-phosphate synthase (its purification and characteristics)].

Pig thyroid myoinositol-phosphate synthase was purified about 30 times using ammonium sulphate fractionation and DEAE cellulose chromatography. The enzyme preparation showed the activity of more than 70 mU/mg of protein. A partially purified synthase is a very labile enzyme. Its activity showed optimum value at pH 7.0. This activity appeared to be controlled by NH4+, Na+, and Li+ ions. The biological role of thyroid synthase has been discussed.

Animals↗