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Biomedical subjects

P Kraus

Publications and source records attributed to P Kraus.

At least 55 records · Page 3Linked to original sources
PubMed1987

Local hemostasis in subarachnoid hemorrhage.

Fibrinopeptide A (FPA), platelet-secreted protein, platelet factor 4 and beta-thromboglobulin were determined in the cerebrospinal fluid of patients who had suffered from subarachnoid hemorrhage and were treated with 6 g tranexamic acid or 4 million KIU aprotinin to prevent rebleeding. Platelet-secreted proteins and FPA were cleared from the cerebrospinal fluid within 3 days after bleeding. Their vasoactive and thrombotic capability is limited to the initiation period of vasospasm that usually comes to clinical observation 3-8 days after bleeding. Increased thrombotic activity of the cerebrospinal fluid, as reflected by high levels of FPA and platelet-secreted protein, seemed to promote the occurrence of neurological deficits.

Fibrinogen↗
PubMed1986

Mitochondrial glutathione transferases. The alkylation of mitochondrial membrane yields a catalyst with glutathione-transferase-like properties.

The pretreatment of rat liver mitochondria with alkylating agents (N-ethylmaleimide, iodoacetamide or vinyl pyridine) increased the activity of mitochondrial glutathione transferase (GST) by 100-250%. Further experiments provided evidence that mitochondrial membranes contain an enzymatically inactive protein which can be alkylated through its sulfhydryl groups. By alkylation, this protein achieves catalytic properties similar to those of native GST.

Alkylating Agents↗
PubMed1984

Glutathione S-transferases in chemically induced tumors.

Rats were treated with N-nitrosomorpholin and subsequently with phenobarbital. After several weeks of phenobarbital treatment, foci of altered cells and tumors developed in the livers of the animals. In liver tumors, the activity of glutathione S-transferase was higher than in the surrounding tissue and remained elevated even after the withdrawal of the promoter. Like the glutathione S-transferase from normal liver, tumor glutathione S-transferase activity is composed of several, predominantly basic, isoenzymes with an apparent molecular weight of approximately 45,000.

Animals↗
PubMed1984

Isoenzyme patterns of soluble glutathione S-transferases from rat adrenal gland and ovary.

Soluble glutathione S-transferases (EC 2.5.1.18) of rat adrenal gland and ovary were separated by means of chromatofocusing. Four isoenzymes were found in the former and five in the latter organ. Most adrenal and ovarian GST are basic proteins with an apparent molecular mass of about 45 000. Some of them possess a weak delta 5-ketosteroid isomerase (EC 5.3.3.1) activity, too. The most abundant ovarian GST isoenzyme (iP = 9, 5) has common immunological determinants with the hepatic GST-B.

Adrenal Glands↗
PubMed1983

Purification and some properties of four glutathione-S-transferase isoenzymes from rat testes.

Two anionic and two cationic glutathione-S-transferase (GST) isoenzymes were found in rat testes and purified to electrophoretic homogeneity. The enzymes are heterodimers with molecular weights of about 44 000 daltons and with widely overlapping specifities for electrophilic substrates. Only one isoenzyme yielded a positive immunoprecipitation reaction with antiserum against hepatic GST-B. The reactions with antiserum against hepatic GST-A were all negative. The Michaelis and association constants for some substrates were also determined.

Animals↗
PubMed1980

The activity of glutathione-S-transferases in various organs of the rat.

The activity of glutathione-S-transferases for five electrophilic substrates was measured in ten organs of the rat. Highest activity was found in the liver and steroidogenic organs. The activity in the heart, brain, spleen and lung was relatively low or nil for most substrates.

Adrenal Glands↗
PubMed1980

Resolution, purification and some properties of three glutathione transferases from rat liver mitochondria.

From the matrix of rat liver mitochondria, three GSH transferases were isolated and named Transferase 1, 2.1 and 2.2. Transferases 1 and 2.2 were purified to electrophoretic homogeneity. Transferase 1 contributes up to about 90% of the total mitochondrial GSH-transferring activity. It has a molecular weight of approx. 45 000 and is composed of two subunits of similar size. The isoelectric point is at pH 7.1-7.4. The Km values for GSH and 1-chloro-2,4-dinitrobenzene are 0.3 and 0.7 mmol/l respectively. Transferase 2.2 has the same molecular weight and subunit structure like the Transferase 1 and an isoelectric point at pH 4.8. The apparent Km values for GSH and 1-chloro-2,4-dinitrobenzene are 0.3 mmol/l and 0.4 mmol/l respectively. Transferase 2.1 contributes only 1% of the total mitochondrial GSH-transferring activity. It has high apparent Km values for both GSH and 1-chloro-2,4-dinitrobenzene (5.6 mmol/l and 1.3 mmol/l resp.) and a limited spectrum of substrates.

Animals↗
PubMed1979

Particle-bound glutathione-S-transferases.

The incubation of liver microsomes or mitochondria with glutathione, in the presence of electrophilic compounds, decreased the glutathione concentration in the incubation medium. Product analysis revealed that glutathione conjugates were formed.

Animals↗