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Biomedical subjects

H W Goedde

Publications and source records attributed to H W Goedde.

At least 91 records · Page 5Linked to original sources

Population genetic studies in three Chinese minorities.

Three minority ethnic groups from China (Mongolians, Koreans, Zhuang) were examined with respect to the genetic markers GLO, GPT, ACP, ESD, 6-PGD, PGM1 subtypes, C3, and TF. Significant variations were noted for the gene frequencies of GLO, GPT, ESD, sub PGM1 between Zhuang and Mongolians; for GPT, ACP, ESD, sub PGM1 between Zhuang and Koreans; and for GLO between Mongolians and Koreans.

Adolescent↗

Erythrocyte and HLA antigens of Atacameño Indians.

The present study reports the results of erythrocyte antigen typing for the following systems: ABO, MN, Rh, Kell, Duffy, and Diego in roughly 180 Atacameño Indians from the oasis of Toconao, northern Chile. A subsample was tested for variation at the histocompatibility loci A, B, and C. Results agree with previous findings based on smaller samples. Caucasian admixture of the Atacameño from Toconao was estimated to be 0.056 +/- 0.022.

Blood Group Antigens↗

Ecogenetic studies in Atacameño Indians.

Aldehyde dehydrogenase deficiency, N-acetyltransferase variation and the polymorphisms of alpha 1-antitrypsin, serum cholinesterase, paraoxonase, and delta-aminolevulinic acid dehydratase were investigated in 180 Atacameño Indians from the North of Chile. The genetic predisposition of these individuals for possible atypical reactions against environmental agents and drugs, as well as general implications of these findings, are discussed.

Aldehyde Oxidoreductases↗

Cytogenetic effects of paraoxon and methyl-parathion on cultured human lymphocytes: SCE, clastogenic activity and cell cycle delay.

Paraoxon and methyl-parathion (Wofatox), frequently used organophosphate pesticides, were tested for cytogenetic effects in lymphocytes of persons with different phenotypes of paraoxonase activity. Sister chromatid exchanges (SCE), chromosome breaks, and cell cycle traverse were studied in ten individuals. Paraoxon showed no significant effects whereas methyl-parathion showed a dose-dependent increase in the SCE and a definite delay in the cell cycle as assessed by fluorescence plus Giemsa technique. No significant clastogenic effects and no difference in response were observed among individuals with different phenotypes of paraoxonase.

Aryldialkylphosphatase↗

Aldehyde dehydrogenase isozyme deficiency and alcohol sensitivity in four different Chinese populations.

Four different populations of China were studied regarding aldehyde dehydrogenase isozyme variation and incidence of alcohol sensitivity. While Korean and Mongolian minorities in the north showed an isozyme I deficiency with a frequency of about 25 and 30%, 45-50% of Zhuang and Han were deficient, respectively. Adverse reactions after alcohol drinking were mainly reported by those subjects who showed the lack of aldehyde dehydrogenase isozyme I.

Aldehyde Dehydrogenase↗

Aldehyde dehydrogenase isozymes in stomach autopsy specimens from Germans and Chinese.

Human stomach aldehyde dehydrogenase (ALDH) isozymes were screened in random autopsy specimens from 66 North German and 33 Chinese individuals. Three ALDH isozymes were identified, which differed in their electrophoretic mobility, affinity to acetaldehyde, propionaldehyde, furfural, and to NAD+ as coenzyme as well as in inhibition by disulfiram, pH optimum and heat stability. While all the German stomach specimens showed ALDH I, ALDH II, and ALDH III isozymes, these isozymes were found in 68, 88, and 99% of the Chinese samples, respectively. The electrophoretic resolution of ALDH III into different activity bands is apparently due to the artefactual formation of secondary isozymes rather than to the existence of genetic variants.

Aldehyde Dehydrogenase↗

Studies in fibroblasts of patients with the Lesch-Nyhan syndrome and HPRT variants. Correlation of HPRT activity with hypoxanthine utilization and growth in selection media.

In the present study, hypoxanthine phosphoribosyltransferase (HPRT) has been investigated in fibroblasts of 19 patients from 16 different families with HPRT deficiency, concerning activity, incorporation of 14C-hypoxanthine, and growth in 8-azaguanine and HAT (hypoxanthine, azaserine, thymidine containing) selection media. According to these data we could classify the patients into 5 groups (patients with classical Lesch-Nyhan syndrome and patients with HPRT variants of types A, B, C, D). In 3 groups (patients with classical Lesch-Nyhan syndrome, HPRT variants C and D), a correlation of residual HPRT activity with the incorporation of 14C-hypoxanthine as well as growth in 8-azaguanine and HAT selection was observed. The variant A, from a patient with the classical Lesch-Nyhan syndrome, exhibited higher HPRT activity than that from all the other patients with the Lesch-Nyhan syndrome. However, the values of hypoxanthine incorporation and growth in selection media were as in the classical syndrome. The cells of variant B were resistant to azaguanine and grew in HAT selection media in the range of control cells, but had HPRT residual activities similar to those of variants A and C. For the characterization of the genetic heterogeneity of HPRT, it seems necessary to study the enzymatic properties in cell extracts as well as the purine uptake and proliferation of cells in different selection media.

Azaguanine↗

Plasma alcohol dehydrogenase in normal and alcoholic individuals.

Determination of plasma alcohol dehydrogenase (ADH) in patients with alcohol-related disorders may be a valuable diagnostic and prognostic parameter. By using a sensitive spectrophotometric method we have measured the plasma ADH activity in chronic alcoholics, non-alcoholic psychiatric patients and healthy blood donors from Germany. Serum alanine aminotransferase (GPT) and serum gamma-glutamyltransferase (gamma-GT) values were included for the comparative study to assess the extent of hepatic complications. The results indicate that plasma ADH activity in alcoholics and non-alcoholic psychiatric patients was significantly raised only when higher GPT and gamma-GT values were observed, which may hint at a generalized liver damage. It is suggested that plasma ADH determination alone is not useful as a diagnostic marker of alcoholism but could be of value when measured in combination with other biochemical parameters.

Alanine Transaminase↗

Two-dimensional electrophoresis of soluble and structure-bound proteins from cultured human fibroblasts and hair root cells: qualitative and quantitative variation.

Proteins from cultured human fibroblasts and native human hair root cells were investigated using the two-dimensional electrophoresis (2DE) technique. Cell material from 35 different healthy persons was examined. Proteins of different sources were separated: total proteins of fibroblasts (12 cell lines), soluble proteins of fibroblasts (12 cell lines), structure-bound proteins of fibroblasts (eight cell lines) and soluble proteins of hair root cells (12 subjects). The protein samples of different individuals were run in pairs through the electrophoresis procedure and the two patterns of each pair were compared. All changes in the electrophoretic mobility of polypeptide spots (qualitative variants) and all clearly visible differences in the staining intensity of the spots (quantitative variants) were scored. Less than 1% of the qualitative variants per pattern was found in total cell proteins and this percentage was not increased in soluble proteins. No qualitative variation was detected in structure-bound proteins. Quantitative variation occurred to a considerably higher degree in the 2DE patterns than qualitative changes. The incidence of quantitative variants was about three times higher in soluble proteins (11%) than in structure-bound proteins (3.5%); in the total cell proteins it lay in between (7%). Cultured cells (fibroblasts) and native cells (hair root cells) showed a similar degree of variation. A comparison of the data shown here with data obtained by an investigation on inbred strains of the mouse suggest that the major part of the quantitative variants observed in the 2DE patterns of proteins were genetically determined. The results presented here and the mouse data mentioned above lead us to the conclusion that the genetic variability of proteins may be characterized by quantitative changes rather than by qualitative changes, and that the genetic variability occurs to quite different degrees in different classes of proteins: structure-bound proteins less than soluble non-enzymatic proteins less than enzymes (certain groups).

Adolescent↗

Cytogenetic effects of acetaldehyde in lymphocytes of Germans and Japanese: SCE, clastogenic activity, and cell cycle delay.

Acetaldehyde, the first metabolite of ethanol oxidation, caused a dose-dependent linear increase in the induction of sister chromatid exchanges in lymphocytes from both Germans and Japanese. Japanese, possessing only aldehyde dehydrogenase II isozyme (ALDH I deficient phenotype) and showing adverse effects after alcohol ingestion, did not differ in SCE rates from Germans and Japanese possessing isozymes I and II. At acetaldehyde concentrations above 360 microM, a significant chromosome breaking effect and a definite delay in cell cycle events, as evaluated by the BdUrd labeling technique, was registered in all individuals. Pyridoxal 5'-phosphate showed no protective effect against acetaldehyde-induced SCE formation in our system. A 24-h extension of the normal culture period revealed significantly higher rates of SCE at acetaldehyde doses above 360 microM.

Acetaldehyde↗

Amino acid sequence of the active site of human pseudocholinesterase.

The usual E1u and atypical E1a human pseudocholinesterases (acylcholine acylhydrolase, EC 3.1.1.8) were purified to homogeneity. The active-site serine residue was conjugated with diisopropyl fluorophosphate and digested with trypsin. The tryptic peptide containing the active site was isolated by gel filtration followed by two-dimensional paper chromatography and electrophoresis. The amino acid sequence of the active site peptide obtained from the usual E1u enzyme was found to be Gly-Glu-Ser-Ala-Gly-Ala-Ser-Ala-Val-Ser-Leu. A remarkable structural homology exists between the human and the horse enzymes in their active sites. From the difference in electrophoretic mobility of the active-site peptides obtained from the usual and atypical enzymes, the probable structure of the atypical human enzyme was deduced as Gly-His-Ser-Ala-Gly-Ala-Ser-Ala-Val-Ser-Leu.

Amino Acid Sequence↗

Comparative study of erythrocyte aldehyde dehydrogenase in alcoholics and control subjects.

Human erythrocyte aldehyde dehydrogenase (ALDH, EC 1.2.1.3) shows a single activity band on starch gel electrophoresis and isoelectric focusing in polyacrylamide gel (pI = 5.0-5.3). The erythrocyte enzyme is identical with the slower migrating, disulfiram-sensitive human liver ALDH isozyme II. Significantly decreased activity of erythrocyte ALDH was observed in chronic alcoholics when compared with healthy controls and non-alcoholic psychiatric and gastrointestinal patients. The measurement of ALDH in erythrocyte lysates may offer yet another sensitive and specific biochemical marker of alcoholism.

Alcoholism↗

Blood ethanol and acetaldehyde levels in Japanese alcoholics and controls.

Aldehyde dehydrogenase (ALDH) isozyme I deficiency in hair root samples from 105 healthy individuals and 72 alcoholics was determined using isoelectric focusing. From these individuals, 12 male alcoholics (2 with ALDH isozyme I deficiency and 10 normal) and 45 healthy controls (18 with ALDH isozyme I deficiency and 27 normal) were investigated for their blood ethanol and acetaldehyde levels by gas chromatography after an acute dose of alcohol (0.5 g ethanol/kg body wt.). Peak blood ethanol values of about 10 mmol/l were attained after 1 hour both in alcoholics and normal controls irrespective of their ALDH type. There was no significant difference in the blood ethanol level during the 5 hr post-drinking period in both the groups. Peak blood acetaldehyde concentration was significantly higher in healthy controls and alcoholics deficient in ALDH isozyme I after alcohol drinking (about 30 micro-mmol/l) than in individuals with normal ALDH isozyme I (3 micro-mmol/l). However, no significant difference in blood acetaldehyde was observed between alcoholics and controls.

Acetaldehyde↗

Aldehyde dehydrogenase isozyme variation and alcoholism in Japan.

Aldehyde dehydrogenase (ALDH) isozyme composition in hair roots was determined using isoelectric focusing in 105 healthy individuals, 175 alcoholics, 86 schizophrenics and 47 drug dependents. The incidence of ALDH isozyme I deficiency in healthy populations in Japan was found to be about 40%. Among alcoholics, however, only 2.3% individuals had the isozyme deficiency. There was no difference between normal controls, schizophrenics and drug dependents regarding the incidence of ALDH isozyme I deficiency. These observations indicate a possible protective role of ALDH isozymes against alcoholism. The higher frequency of ALDH isozyme I deficiency in Japanese may explain why alcoholism in Japan has been less frequent than in European and North American countries. ALDH isozyme II was found in most of the tissues and erythrocytes. A higher frequency of individuals possessing lower ALDH activity in hemolysates was observed in alcoholics than that in controls. The activity of acid phosphatase was also reduced in alcoholics. Alcohol abuse might result in disturbed protein synthesis in the erythrocytes.

Acid Phosphatase↗