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H W Goedde

Publications and source records attributed to H W Goedde.

At least 73 records · Page 4Linked to original sources
PubMed1986

Detection and partial characterization of a variant form of cytosolic aldehyde dehydrogenase isozyme.

A rare case of human liver cytosolic aldehyde dehydrogenase (isozyme II) variation discovered in a Chinese autopsy liver specimen is reported. While the major isozyme band was nearly absent, several additional minor bands were observed on isoelectric focusing gel. Rabbit antibodies to purified human liver ALDH II showed immunological cross-reactivity for the variant enzyme bands. The existence of additional minor bands indicates the presence of tetramer hybrid forms made up of normal and variant monomers. The observed abnormality may represent the heterozygous form of ALDH II variation. A similar variant was also detected in erythrocytes of a male Thai student.

Aldehyde Dehydrogenase↗
PubMed1986

Isolation of repetitive clones from human muscle cDNA library.

Human fetal muscle cDNA library was screened with a beta-myosin heavy chain gene fragment containing Alu sequences. Two cDNA clones AI and BII with 1.8 and 3 kb inserts respectively were chosen for further characterization by means of RNA and DNA hybridization procedures and sequencing. The clones appeared to contain repetitive sequences as well as single copy regions. They are actively transcribed in different stages of myogenic development but not in the liver. DNA sequence analysis of short stretches from both clones revealed no sequence homology to any other published DNA sequences.

Base Sequence↗
PubMed1986

delta-Aminolevulinic acid dehydrase (porphobilinogen synthase) in two families with inherited enzyme deficiency.

The inheritance of a deficient delta-aminolevulinic acid dehydrase (ALA-D; synonym: porphobilinogen synthase; EC 4.2.1.24) was studied in blood samples of two families over three generations. The propositus in each family was a young male acute hepatic porphyria patient with an almost complete ALA-D deficiency in the homozygous state (ALA-D activity less than 2% of controls). Heterozygotes are clinically non-affected (mean ALA-D 36% of controls). The mode of transmission could be traced by enzyme activity and electrophoretic polymorphism studies. Heterozygotes are detected by the demonstration of enzyme activity in the gel. The notation D was used for the gene expressing the defective enzyme. The "phenotype" D-1 was observed in six, the "phenotype" D-2 in three of all heterozygotes studied. These results are compatible with a single normal allele in heterozygotes responsible for enzyme activity. Quantitative assays and the segregation pattern in both families suggest a 3-allele-system for the inheritance of ALA-D deficiency.

Alleles↗
PubMed1986

Incidence of specific anosmia in Northern Germany.

Thresholds for the perception of 6 primary odorants were tested in a sample of 153 unrelated healthy individuals including 101 males and 52 females. Using some special precautions and directions for preparing aqueous solutions of primary odorants, screening for specific anosmia was found to be a practicable method with reliable results. The observed perception thresholds showed a bimodal distribution. Individuals with higher values probably are specific anosmics. Relatively lower frequencies of anosmia observed in this sample, as compared to reported values in Caucasians of the USA, are probably due to genetic differences. The pheromone character of some odorants and their possible genetic relevance is discussed.

Adolescent↗
PubMed1986

Aldehyde dehydrogenase polymorphism in North American, South American, and Mexican Indian populations.

While about 40% of the South American Indian populations (Atacameños, Mapuche, Shuara) were found to be deficient in aldehyde dehydrogenase isozyme I (ALDH2 or E2), preliminary investigations showed very low incidence of isozyme deficiency among North American natives (Sioux, Navajo) and Mexican Indians (mestizo). Possible implications of such trait differences on cross-cultural behavioral response to alcohol drinking are discussed.

Aldehyde Dehydrogenase↗
PubMed1985

Dermatoglyphic findings in patients with fragile X-chromosome.

Finger- and palmar prints of hemi- and heterozygote fragile X-patients with mental retardation (10 males and 5 females) were compared to dermatoglyphic findings in 20 mentally retarded patients (10 males and 10 females) without fragile X and to 200 healthy unrelated persons (100 males and 100 females). Characteristic whorls and double-loops with high ridge-counts on finger-tips and a pronounced transversal course of palmar ridges were restricted to males with fragile X. Female carriers of fragile X showed, corresponding to male patients, some abnormalities of the digital- and palmar ridge-pattern. Contrary to males, in carriers as well as in mentally retarded females without fragile X, fingerprints with low ridge-counts were found. Common to all mentally retarded patients, but more pronounced in males with fragile X, abnormal palmar creases and hand-measurements were observed. These findings probably are related to prenatal retarded growth of the length of the palma and of the middle-finger.

Dermatoglyphics↗
PubMed1985

Human placental aldehyde dehydrogenase. Subcellular distribution and properties.

Freshly obtained human term placentae were subjected to subcellular fractionation to study the localization of NAD-dependent aldehyde dehydrogenases. Optimal conditions for the cross-contamination-free subcellular fractionation were standardized as judged by the presence or the absence of appropriate marker enzymes. Two distinct isozymes, aldehyde dehydrogenase I and II, were detected in placental extracts after isoelectric focusing on polyacrylamide gels. Based on a placental wet weight, about 80% of the total aldehyde dehydrogenase activity was found in the cytosolic acid and about 10% in the mitochondrial fraction. The soluble fraction (cytosol) contained predominantly aldehyde dehydrogenase II which has a relatively high Km (9 mmol/l) for acetaldehyde and is strongly inhibited by disulfiram. The results indicate that cytosol is the main site for acetaldehyde oxidation, but the enzyme activity is too slow to prevent the placental passage of normal concentrations of blood acetaldehyde (less than 1 mumol/l) produced by maternal ethanol metabolism.

Acetaldehyde↗
PubMed1985

Association of N-acetyltransferase polymorphism and environmental factors with bladder carcinogenesis. Study in a north German population.

The N-acetyltransferase phenotype was determined in 105 German patients with bladder carcinoma and in a control group of 42 healthy subjects. The slow phenotype was significantly more frequent among the patients (61.9% compared to 42.9% in the control group). Potential risk factors like occupational exposure, smoking habits, drug abuse and urological anamnestic predispositions were evaluated in relation to staging and grading of the disease, and acetylator phenotype.

Acetyltransferases↗
PubMed1985

Effect of amphetamine on brain catecholamines, brain beta-endorphin, serum prolactin, catechol-O-methyltransferase and monoamine oxidase of various organs in the rat.

Rats were treated with amphetamine to induce an amphetamine psychosis which resembles paranoid schizophrenia. Brain catecholamines, brain beta-endorphin, serum prolactin as well as catechol-O-methyltransferase and monoamine oxidase were subsequently measured. The norepinephrine levels were significantly lower in brain regions of rats treated with amphetamine whereas levels of dopamine and beta-endorphin remained the same. No significant changes were found in the levels of catechol-O-methyltransferase, monoamine oxidase and serum prolactin. In view of recent findings by other investigators in this field, our results suggest an important role of the adrenergic system in the pathogenesis of amphetamine psychosis.

Amphetamine↗