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Biomedical subjects

V Richter

Publications and source records attributed to V Richter.

At least 73 records · Page 4Linked to original sources
PubMed1983

[Adenosine deaminase activity in hemoblastoses].

The activity of adenosine deaminase was determined in lymphocytes, erythrocytes and blood plasma of 73 patients with different haematological malignancies and also in healthy control subjects. The enzyme activities were measured using adenosine as substrate and by analysis of released ammonia. Statistically significant decreased enzyme levels in lymphocytes and partial also in erythrocytes were observed in chronic lymphocytic leukaemia, Hodgkin's disease and multiple myeloma. The lower activities of ADA of these patients may be related to the impaired immunological function. In contrast in myeloid leukaemia, blast crisis of myeloid leukaemia and in acute leukaemias significant increased ADA levels in lymphocytes or blast cells were observed. Between the content of blast cells in peripheral blood and ADA activity of the mononuclear cell fraction exists a positive correlation. The increased ADA values of blast cells are a sign of an elevated purine metabolism.

Adenosine Deaminase↗
PubMed1982

[Adenosine deaminase activity in Hodgkin's disease (author's transl)].

The activity of adenosine deaminase (ADA) (EC3.5.4.4.) was determined in the blood plasma, erythrocytes, and lymphocytes of 23 patients with Hodgkin's disease and partly also in 99 control subjects. The enzyme activities were measured using adenosine as substrate and by analysis of ammonia. No correlation was found between the ADA activities in lymphocytes, erythrocytes, and blood plasma. The lymphocytes of the patients revealed lower ADA activities (U/g protein) than the lymphocytes of control subjects. The ADA activity is not reduced in plasma or erythrocytes. The lower activities of ADA in the lymphocytes of patients may be related to the impaired cell-mediated immunity of the Hodgkin's disease.

Adenosine Deaminase↗
PubMed1981

[Gene expression, metabolic regulation and aging].

The biological ageing comprises changes of of structure and function depending on time with the beginning of the autonomy of a living being up to death. On the one hand, the causes of this process are genetically fixed, on the other hand they depend on environmental factors and are not programmed. In the course of life the total genome and also the nucleic acid underlie influences, which must have consequences on the gene expression. In these cases the changed sensitivity of the genetic apparatus in comparison to hormones is impressionably changed. The decreased protein biosynthesis may be stimulated by increased amino acid concentrations and by SH-substances, Age-depending changes are also observed for enzymatically catalyzed reactions and in the regulation of chains of metabolism. At first the biologic ageing appears as a complex multiform process, which reaches the simplest integration level in the cellular metabolism.

ATP Citrate (pro-S)-Lyase↗
PubMed1981

[Adenosine deaminase activity in leukemia patients].

The activities of adenosine deaminase (ADA) were measured in the blood plasma, erythrocytes, and lymphocytes of healthy reference persons and in patients affected with leukaemia. ADA is increased in patients with acute immature cell leukaemia, in patients with chronic lymphatic leukaemia it is comparatively low in lymphocytes. In chronic myeloic leukaemia ADA activities are different depending on the activity of the disease. ADA-activities in the blood plasma, erythrocytes, and lymphocytes do not correlate with each other. ADA-activities in leukaemias may be regarded as an indicator of increased purin metabolism rather a as parameter of disturbed cellular immunofunction.

Acute Disease↗
PubMed1981

[The age-dependent influence of diet on lipid metabolism (author's transl)].

In contrast to 3 months old rats of the Wistar strain show 18 months old animals an elevation of the serum triglyceride level under the conditions of a sucrose diet (25% of the energy uptake). Clinical investigations with women show a similar age difference. These results may not be explained by the age-dependent behavior of the activity of several lipogenic enzymes of liver and adipose tissue and of their adaptation to a sucrose diet, but the age-dependent decrease of the lipoprotein lipase activity may be of special importance.

Adolescent↗
PubMed1981

[Adaptation of lipogenic enzymes of liver and adipose tissue to starvation and refeeding (author's transl)].

The lipogenic enzymes-6-phosphate dehydrogenase, citrate cleavage enzyme and malic enzyme of both liver and adipose tissue of rate of the wistar strain show a diminished activity in dependence on age. In the liver exists no age difference of the characteristic adaptation under the conditions of starvation and refeeding, but in adipose tissue of 18 months old rats the lipogenic enzymes show a poorer elevation of activity during refeeding after a 48 h period of starvation than in 3 months old animals. The serum inulin level and his variation in starvation and refeeding are independent of age.

Adipose Tissue↗
PubMed1980

[Circadian rhythm and aging].

The circadian variation of several lipogenic enzymes of rat liver and of serum triglyceride and insulin levels was measured in dependence on age. In female rats of the Wistar strain subjected to a 12 hr light--12 hr darkness schedule malic enzyme and isocitrate dehydrogenase show a circadian cycle with maximum activities in the dark period, alpha-glycerophosphate dehydrogenase has a maximum at 14,00 hr. The circadian rhythm of these enzymes is synchronous in young and old animals, but the activities of malic enzyme and alpha-glycerophosphate dehydrogenase are lower in the liver of 18 months old rats in contrast to 3 months old animals at all time points. The activity of glucose-6-phosphate dehydrogenase of the liver of young rats increases during the light period and reaches a maximum at night. The enzyme in old animals does not show this circadian rhythm. There is no age-dependence of the circadian variation of serum triglyceride and insulin levels.

Aging↗
PubMed1980

[lipid metabolism and ageing (author's transl)].

Aging in man and in animals is associated with a variety of changes in lipid metabolism. Age-dependent changes of the lipid metabolisms of liver, adipose tissue and other organs lead to the age dependence of the blood lipid level. Aging organisms synthesize and metabolize less lipids, the result being an age-related increase of lipid in tissues and blood. Both intrinsic aging processes and risk factors (such as hyperlipoproteinemias) operative over many years apparently act to produce the multifactoral age-related disease atherosclerosis.

Adipose Tissue↗
PubMed1980

[HDL/LDL-cholesterol, arteriosclerosis and age (author's transl)].

The level of HDL-Cholesterol of the serum of women decreases in dependence on age. Especially in the group of the 75-95 years old persons. The LDL-cholesterol shows an increase with a maximum in the age group 60-75 years. Thus the HDL/LDL-cholesterol quotient is reduced and the risk for atherosclerotic diseases is elevated. Serum HDL-cholesterol correlates positively with the post-heparin lipolytic activity of extrahepatic origin, but not with the hepatic lipase.

Aged↗
PubMed1980

[Intravasal lipoproteid metabolism and age (author's transl)].

The post-heparin-lipolytic activity of women decreases in dependence on age. This age dependence is the result of a diminished activity of post-heparin-lipase of extrahepatic origin, whereas no age differences of the activities of hepatic lipase exist. There is a negative correlation between serum triglycerides and the post-heparin-lipolytic activity, especially between the enzyme of extrahepatic source and the triglyceride level, but not between the hepatic lipase and triglycerides. Serum-HDL-cholesterol correlated positively with the post-hepatic-lipolytic activity.

Adolescent↗
PubMed1978

[Enzymes of carbohydrate and lipid metabolism in dependence on age (author's transl)].

The levels of the rat liver enzymes glucose-6-phosphate-dehydrogenase, alpha-glycerophosphate-dehydrogenase and citrate cleavage enzyme decrease between the age groups of 3 and 18 months. The half-life time of these enzymes is uneffected by age and the diminished levels of the enzymes in the liver of old rats can be ascribed to a reduced rate of enzyme synthesis. The half-life time of malic enzyme decreases as a function of age and this increased enzyme destruction may contribute to the diminished malic enzyme level of old rat liver.

ATP Citrate (pro-S)-Lyase↗