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Biomedical subjects

E Ziomek

Publications and source records attributed to E Ziomek.

29 records · Page 2Linked to original sources
PubMed1982

Acylases in plasma of hamsters with experimental hepatitis.

After the administration of D-galactosamine to golden Syrian hamsters, a rapid but short-lived increase in acylase I and cobalt-activated (AA-Co) activity was noted in the blood plasma, but not in the liver. In the plasma of control hamsters, only form 2 AA-Co was identified, but during experimental hepatitis, the appearance of form 1 was observed. Only form 2 hamster enzyme is strongly inhibited by alpha-hydroxyisocaproil-tyrosine and reacts with antihuman form 2 antibody.

Alanine Transaminase↗
PubMed1981

Molecular forms of bovine gamma-glutamyltransferase and their enzyme immunoassay.

Light form of bovine kidney gamma-glutamyl transferase was isolated from heavy form of the enzyme after digestion with bromelain. Its apparent molecular weight was 95,000 and in SDS solution it dissociated into two non-identical subunits with molecular weights 26,000 and 69,000. No substantial differences between both forms in activation, kinetic parameters and inhibition with anthglutin and its isomers were noted. Using enzyme immunoassay it was possible to determine one enzyme form in the presence of the other. This was applied for studies of gamma-glutamyltransferase forms in cow serum and colostrum.

Animals↗
PubMed1979

Molecular forms of cobalt-activated acylase in human tissues and serum of patients with viral hepatitis.

Two molecular forms of cobalt-activated acylase present in human tissues and one or three in sera of patients with viral hepatitis were noted. They have different substrate specificity. Only form 2 is strongly inhibited by alpha-hydroxyisocaproyl-tyrosine and -phenylalanine. Electrophoretic migrations of all enzyme forms are different from those of aminoacylase. Immunoglobulin antiform 2 of the acylase does not precipitate other forms of cobalt-activated acylase or aminoacylase.

Aminopeptidases↗
PubMed1979

Properties of penicillin amidase immobilized by copolymerization with acrylamide.

An enzyme preparation in a spherical granule form was obtained by copolymerization of penicillin amidase (EC 3.5.1.11) (previously modified with maleic anhydride) and acrylamide via a crosslinking agent. As compared with the native enzyme, immobilized amidase is more resistant to heating, has a lower affinity to benzylpenicillin, and is less inhibited by phenylacetate. Its substrate specificity and optimum pH remain unchanged.

Acrylamides↗
PubMed1978

Polymorphism of the cobalt-activated acylase in human tissues.

A method was elaborated for obtaining polyacrylamide gel zymograms of the cobalt-activated acylase after electrophoresis. Two fractions of the acylase showing activity towards N-chloroacetyl-gamma-L-glutamyl-beta-naphthylamide were found in human kidney, liver and intestine. The two fractions isolated from liver differ in substrate specificity, heat resistance, response to metal ions, inhibition by deaminated dipeptides, and in molecular weight. They differ also from other N-acylamino acid amidohydrolases: aminoacylase (EC 3.5.1.14) and aspartoacylase (EC 3.5.1.15).

Aminopeptidases↗
PubMed1978

Activity and polymorphism of the cobalt-activated acylase in tissues of rodents during development.

The activity of cobalt-activated acylase, measured towards N-chloroacetyl- and N-butyryl-gamma-L-glutamyl-beta-naphthylamide, was found in all tissues of the adult animals. In the kidney, liver and small intestine of adult guinea-pig and rat two fractions differing in electrophoretic mobility (fractions 1 and 2) were present. The early foetus contained fraction 2, sometimes accompanied by fraction 3 which later disappeared; on further development of the foetus, fraction 1 appeared. Fraction 1 was distinctly activated by cobalt ions; fractions 2 and 3 were strongly inhibited by deaminated leucylphenylalanine. In the guinea-pig, the molecular weight of the three fractions ranged from 43000 to 59000.

Animals↗