Biomedical subjects

H Stelmach

Publications and source records attributed to H Stelmach.

4 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↗

PubMed1965

Single-step stability studies.

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Chemical Phenomena↗

PubMed1965

Release of a drug from a dosage form.

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Aspirin↗

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↗