PubMed Health⌕ Search

Biomedical subjects

E Arndt

Publications and source records attributed to E Arndt.

At least 19 recordsLinked to original sources
PubMed2005

Effect of a barley breakfast cereal on blood glucose and insulin response in normal and diabetic patients.

Prowashonupana (Prowash) is a shrunken-endosperm, short awn, waxy starch, hulless barley with low starch, high fiber, high protein, and a relatively high concentration of free sugars. The study was designed to compare equivalent breakfast meals (w/w) of Prowash and oatmeal for glycemic response in diabetic and non-diabetic subjects. A commercial liquid meal replacer (LMR) was included as a reference standard. A substantial reduction of the post-prandial glycemic peak following ingestion of Prowash was observed as compared to LMR or oatmeal. In the non-diabetic subjects, the maximal rise in glucose from baseline was 26.3 +/- 3.9 mg/dL after LMR, 41.3 +/- 3.9 mg/dL after oatmeal and 6.4 +/- 2.7 mg/dL after Prowash (p < 0.01). The maximal increase in glucose in the diabetic patients was 69.9 +/- 4.5 mg/dL after LMR, 80.8 +/- 8.8 mg/dL after oatmeal and 28.4 +/- 3.5 mg/dL after Prowash (p < 0.01). The maximal increase in insulin post-LMR was 33.9 +/- 3.6 mIU/ml in the diabetic patients and 54.0 +/- 9.8 mIU/ml in the non-diabetic controls. Oatmeal elicited a maximal insulin increase of 29.9 +/- 4.2 mIU/ml in the control subjects and 21.4 +/- 2.5 mIU/ml in the diabetic patients. In contrast, the maximal insulin increase after Prowash was 8.6 +/- 1.5 mIU/ml in the non-diabetic controls and 6.8 +/- 1.2 mIU/ml in the diabetic patients (p < 0.01).

Avena↗
PubMed2001

[Can follow-up controls improve the accuracy of MR mammography? A retrospective analysis of MR mammography follow-up studies].

PURPOSE: To assess the change in diagnostic confidence between first and follow-up dynamic MR examination of the breast (MRM). METHODS: The reports of a total of 175 MRM in 77 patients (mean age 50 years; 36-76) with 98 follow-up MRM were analyzed. All examinations were performed as a dynamic study (Gd-DTPA, 0.16 mmol/kg; 6-7 repetitive studies). The change in diagnostic confidence was retrospectively classified as follows: controlled lesion vanished during follow-up (category I); diagnostic confidence increases during follow-up (II), more likely benign (IIa), more suspicious (IIb); no difference in diagnostic confidence (III). Long-term follow-up over an average of four years was obtained for 57 patients with category IIa/III findings. RESULTS: In 98 follow-up examinations, only two lesions vanished (2%). In 77/98 cases a category IIa lesion was diagnosed, in 11 cases a category IIb lesion. In 8 cases (8%) there was no change in diagnostic confidence during follow-up. Lesions in category IIb underwent biopsy in 10/11 cases, in one case long-term follow-up proved a completely regredient inflammatory change. In 8/11 suspicious findings (IIb) a malignant tumor was detected. The mean time interval between first and follow-up MRM was 8 months for I-IIb lesions, and 4 months for category III lesions. In the long-term follow-up two patients with a category IIa lesion developed a carcinoma in a different breast area after four and five years. CONCLUSION: MRM follow up increases the diagnostic confidence if the time interval is adequate (> 4 months). A persistently or increasingly suspicious finding warrants biopsy.

Adult↗
PubMed1992

Nucleotide sequence of the genes for ribosomal proteins HS15 and HSH from Haloarcula marismortui: an archaeon-specific gene cluster.

The nucleotide sequences of the genes for two ribosomal proteins, HS15 and HSH, from the archaeon Haloarcula marismortui, have been determined. The genes were found in a cluster together with another open reading frame with a probable regulatory function. HS15 and HSH have counterparts in eucarya. HS15 is significantly homologous to S19 from frog (Xenopus laevis). HSH is related to S37 from yeast (Saccharomyces cerevisiae) and S27 from fly (Drosophila melanogaster), as well as to other members of the S27 family. Eubacterial counterparts were not found, suggesting that these proteins are 'extra proteins' that are absent in eubacterial ribosomes.

Amino Acid Sequence↗
PubMed1992

The alpha-operon equivalent genome region in the extreme halophilic archaebacterium Haloarcula (Halobacterium) marismortui.

The genome region of the extreme halophilic archaebacterium Haloarcula marismortui equivalent to the alpha-operon of Escherichia coli has been characterized. In H. marismortui, the alpha-operon was found to be located immediately upstream from the S9 gene cluster. The gene order in the halobacterial alpha-operon, given according to the gene products, is tRNA(Ser), HmaS13, HmaS4, HmaS11, and HmaRp alpha. Compared to the corresponding operon from E. coli, the halobacterial gene organization differs in (i) the presence of a gene for tRNA(Ser) (GCU), (ii) the reversed order of the genes for the ribosomal proteins HmaS11 and HmaS4, and (iii) the absence of the gene coding for the ribosomal protein L17. The primary structure of HmaRp alpha shows high similarity to a subunit of eukaryotic RNA polymerase II (YeaRpB3, HsaRpB33), whereas the similarity to the eubacterial alpha-subunit of RNA polymerase is only weak.

Amino Acid Sequence↗
PubMed1992

The genes for ribosomal protein L15 and the protein equivalent to secY in the archaebacterium Haloarcula (Halobacterium) marismortui.

The nucleotide sequences of the L15 gene and the secY gene, which form the last two genes of the S10/spc-operon region of Haloarcula marismortui, have been determined. The HmaL15 protein sequence translated from the DNA is 164 amino acids long, revealing 10 amino acids more at the C-terminus than the published protein sequence. The deduced HmasecY protein sequence has 487 amino acids and shows significant homology to its counterparts in Methanococcus vannielii and Escherichia coli. The gene order of the halobacterial gene cluster is similar to that in the methanogens and in eubacteria.

Amino Acid Sequence↗
PubMed1991

Halobacterial S9 operon. Three ribosomal protein genes are cotranscribed with genes encoding a tRNA(Leu), the enolase, and a putative membrane protein in the archaebacterium Haloarcula (Halobacterium) marismortui.

In the eubacterium Escherichia coli the genes for the ribosomal proteins L13 and S9 form an operon consisting of two genes. The corresponding operon of the archaebacterium Haloarcula marismortui (Halobacterium marismortui was recently reassigned to the genus Haloarcula [Oren, A., Ginzburg, M., Ginzburg, B. Z., Hochstein, L. I., and Volcani, B. E. (1990) Int. J. Syst. Bacteriol. 40, 209-210] and is now called Haloarcula marismortui) which is presented here, is much larger encoding three ribosomal proteins (HL29, HmaL13, HmaS9), a tRNA(Leu), the glycolytic enzyme enolase (HmaEno), a putative membrane protein (OrfMSG), and two not yet identified open reading frames (OrfMMV, OrfMNA). The nucleotide sequence of 3931 base pairs has been established. Northern analysis revealed the existence of a polycistronic mRNA (3.7 kilobases) demonstrating that the transcription of a gene of the glycolytic pathway is coupled to the transcription of ribosomal protein genes. Upstream of the first gene of the operon (tRNA(Leu)) a promoter structure typical for the extreme halophilic archaebacteria was detected and downstream of the last gene (OrfMSG) a terminator structure was present. As shown by S1-nuclease mapping, a tRNA-mRNA transcript as well as the mRNA alone was present in vivo. The transcriptional start point and the tRNA-mRNA cleavage point are shown to be almost identical to the 5' and 3' ends, respectively, of the putative mature tRNA. The C-terminal part of the OrfMSG protein shows a significant similarity to the vertebrate laminin receptor protein.

Bacterial Proteins↗
PubMed1991

Organization and nucleotide sequence of ten ribosomal protein genes from the region equivalent to the spectinomycin operon in the archaebacterium Halobacterium marismortui.

The nucleotide sequence has been determined of a 4700 bp region from a ribosomal protein gene cluster of Halobacterium marismortui (Haloarcula marismortui), which is equivalent to part of the spectinomycin operon of Escherichia coli. The genes were localized on the recombinant lambda EMBL3 clone PP*7, which also contains several other ribosomal protein genes from the DNA region in H. marismortui equivalent to the linked S10/spc operon. The genes analysed encode ten ribosomal proteins, namely HmaL5, HmaS14, HmaS8, HmaL6, HL5, HL24, HmaL18, HmaS5, HmaL30 and HmaL15. The gene organization of the archaebacterial cluster is similar to that in eubacteria but has two additional genes, namely those encoding HL5 and HL24, which were identified as extra proteins that are apparently not present in E. coli. These correspond to the gene products of orfd and orfe in Methanococcus vannielii and also have eukaryotic counterparts.

Amino Acid Sequence↗
PubMed1991

Primary structures of ribosomal proteins from the archaebacterium Halobacterium marismortui and the eubacterium Bacillus stearothermophilus.

Approximately 40 ribosomal proteins from each Halobacterium marismortui and Bacillus stearothermophilus have been sequenced either by direct protein sequence analysis or by DNA sequence analysis of the appropriate genes. The comparison of the amino acid sequences from the archaebacterium H marismortui with the available ribosomal proteins from the eubacterial and eukaryotic kingdoms revealed four different groups of proteins: 24 proteins are related to both eubacterial as well as eukaryotic proteins. Eleven proteins are exclusively related to eukaryotic counterparts. For three proteins only eubacterial relatives-and for another three proteins no counterpart-could be found. The similarities of the halobacterial ribosomal proteins are in general somewhat higher to their eukaryotic than to their eubacterial counterparts. The comparison of B stearothermophilus proteins with their E coli homologues showed that the proteins evolved at different rates. Some proteins are highly conserved with 64-76% identity, others are poorly conserved with only 25-34% identical amino acid residues.

Amino Acid Sequence↗
PubMed1990

Evidence for an additional archaebacterial gene cluster in Halobacterium marismortui encoding ribosomal proteins HL46e and HL30.

A small and extremely basic ribosomal protein (HL46e) has been purified from Halobacterium marismortui using reversed-phase high-performance liquid chromatography (HPLC). The amino acid sequence of the protein was determined by automated N-terminal and internal sequence analysis. Comparison of this sequence with other ribosomal protein sequences from eubacteria, archaebacteria and eukaryotes revealed a strong homology to SL46e from Sulfolobus solfataricus, YeaL46 from yeast and RL39 from rat. No significant sequence similarly was found to any eubacterial ribosomal protein so far known. Using a specific oligonucleotide probe the HL46e gene was identified, cloned and the nucleotide sequence including the 5'- and 3'-flanking regions were analysed. The HL46e gene is followed by the gene coding for HL30. A putative halobacterial promoter sequence with the motive 'TTTAAA' has been localized 32 bp upstream of the HL46e gene and a putative terminator sequence localized downstream from the HL30 gene. An equivalent to this HL46e/HL30 operon is apparently not present in Escherichia coli.

Amino Acid Sequence↗
PubMed1990

Nucleotide sequence of four genes encoding ribosomal proteins from the 'S10 and spectinomycin' operon equivalent region in the archaebacterium Halobacterium marismortui.

Four genes encoding ribosomal proteins HmaS17, HmaL14, HmaL24 and HS3, have been identified in the lambda EMBL3 clone PP*7 from a genomic library of the archaebacterium Halobacterium marismortui. The clone contains genes from the 'S10 and spectinomycin' operon equivalent region. Three of the deduced proteins are homologous to the corresponding Escherichia coli and Methancoccus vannielii S17, L14 and L24 proteins, as well as to eukaryotic proteins from rat or yeast. HS3 was identified as an extra protein corresponding to the gene product for orfc in M. vannielii and the eukaryotic ribosomal protein RS4 from rat. The equivalence of HmaL24 (HL16) and E. coli L24, which share only 28% identical amino acid residues, could now be shown by localizing the HmaL24 gene at the same position in the cluster.

Amino Acid Sequence↗
PubMed1990

Organization and nucleotide sequence of a gene cluster coding for eight ribosomal proteins in the archaebacterium Halobacterium marismortui.

A DNA fragment containing the genes for the eight ribosomal proteins HmaL3, HL6, HmaL23, HmaL2, HmaS19, HmaL22, HmaS3, and HmaL29 from Halobacterium marismortui has been cloned and sequenced. The organization of this gene cluster in general corresponds to the S10 operon of Escherichia coli although there exists some differences between them. The sequence analysis of the 5'- and 3'-region of the gene cluster revealed three open reading frames (orf1, orf2, and orf3) which do not code for any ribosomal protein whose structure is known. A putative promoter is located upstream of orf1. Out of the eight ribosomal proteins five have counterparts in eubacteria only, two in both eubacteria and eukaryotes, and one is exclusively related to an eukaryotic ribosomal protein.

Amino Acid Sequence↗
PubMed1989

Ribosomal proteins in halobacteria.

The amino acid sequences of 16 ribosomal proteins from archaebacterium Halobacterium marismortui have been determined by a direct protein chemical method. In addition, amino acid sequences of three proteins, S11, S18, and L25, have been established by DNA sequencing of their genes as well as by protein sequencing. Comparison of their sequences with those of ribosomal proteins from other organisms revealed that proteins S14, S16, S19, and L25 are related to both eukaryotic and eubacterial ribosomal proteins, being more homologous to eukaryotic than eubacterial counterparts, and proteins S12, S15, and L16 are related to only eukaryotic ribosomal proteins. Furthermore, some proteins are found to be similar to only eubacterial proteins, whereas other proteins show no homology to any other known ribosomal proteins. Comparisons of amino acid compositions between halophilic and nonhalophilic ribosomal proteins revealed that halophilic proteins gain aspartic and glutamic acid residues and significantly lose lysine and arginine residues. In addition, halophilic proteins seem to lose isoleucine as compared with Escherichia coli ribosomal proteins.

Amino Acid Sequence↗
PubMed1989

Facial reconstruction in Down syndrome: perceptions of the results by parents and normal adolescents.

Randomized videotaped samples of conversational speech recorded preoperatively and 6 months postoperatively in 15 patients with Down syndrome who had undergone facial reconstruction were studied. The videotapes were rated by 34 normal adolescent students for appearance, friendliness, intelligence, and speech. In addition, the opinions of the patients' parents regarding their child's appearance and speech were surveyed. Results indicated that, although most parents reported improvements in their child's speech and appearance, independent raters could not readily discern improvement in any of the four areas studied. The use of videotape recordings to assess improvements in these traits after surgery in children with Down syndrome has not been previously reported.

Adolescent↗
PubMed1988

Molecular cloning and nucleotide sequence of the gene for the ribosomal protein S11 from the archaebacterium Halobacterium marismortui.

The gene encoding ribosomal protein S11 (Escherichia coli S15 homologue) from Halobacterium marismortui was cloned employing two synthetic oligonucleotide mixtures, 23 and 32 bases in length, as hybridization probes. The nucleotide sequence of the gene and the adjacent 5'- and 3'-flanking regions (1300 base pairs) were then determined by the dideoxy chain termination method. Comparison of the nucleotide sequence of the H. marismortui S11 gene with that of the E. coli S15 gene (rpsO) showed that the 3'-end of the S11 gene can be aligned with the entire E. coli S15 gene, sharing 44% identical nucleotides. It has been found that the S11 gene has a higher G + C content (G + C = 65%) than that of the E. coli S15 gene (G + C = 53%). This increase in G + C content specifically shows up as a preference for G + C in the 3rd position of the codon. Upstream of the S11 gene, an archaebacterial promoter sequence (GGACTTTCA) and a putative ribosomal binding site (GCGGT) have been found, 88 and 15 (or 24) base pairs from the initiation codon of the gene. In addition, an open reading frame could be identified immediately after the stop codon for the S11 gene. Northern blotting analysis using the S11 coding region as probe has shown that the S11 gene is located on a 2.4-kilobase mRNA, suggesting that it is cotranscribed with other downstream gene(s).

Amino Acid Sequence↗
PubMed1987

Primary structures of three highly acidic ribosomal proteins S6, S12 and S15 from the archaebacterium Halobacterium marismortui.

The amino acid sequences of three extremely acidic ribosomal proteins, S6, S12, and S15, from Halobacterium marismortui have been determined. The sequences were obtained by the sequence analysis of peptides derived by enzymatic digestion with trypsin. Stapylococcus aureus protease and chymotrypsin, as well as by cleavage with dilute HCl. The proteins, S6, S12 and S15, consist of 116, 147 and 102 amino acid residues, and have molecular masses of 12,251, 16,440 and 11,747 Da, respectively. Comparison of the amino acid sequences of these proteins with ribosomal protein sequences of other organisms revealed that halobacterial protein S12 has homology with the eukaryotic protein S16A from Saccharomyces cerevisiae, while S15 is significantly related to the Xenopus laevis S19 protein. No homology was found between these halobacterial proteins and any eubacterial ribosomal proteins.

Amino Acid Sequence↗