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  • 1
    Electronic Resource
    Electronic Resource
    Gradient High Performance Liquid Chromatographic Assay for Degradation Products of Adinazolam Mesylate in a Sustained Release Tablet Formulation (1995)
    Springer
    Pharmaceutical research 12 (1995), S. 738-745 
    Details
    ISSN: 1573-904X
    Keywords: adinazolam mesylate ; gradient reversed-phase liquid chromatography ; mass spectrometry ; decomposition products assay
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract A gradient high performance liquid chromatographic method was developed to determine degradation products of adinazolam mesylate in a sustained release tablet formulation. Sample preparations were chromatographed on a YMC-Basic column using a formate buffer/acetonitrile gradient with absorbance detection at 254 nm. Adinazolam mesylate was found to degrade at high relative humidity and temperature to form a major product, the 6-aminoquinoline analog, plus numerous other compounds. Five of these compounds were identified and their structures indicate that the solid-state degradation of adinazolam, in the presence of sufficient moisture, involves not only a hydrolytic mechanism, but also an oxidative mechanism. Potential process impurities were resolved from the drug and degradation products. Recovery was near 100% over the 0.5 to 10% range for the major degradate (6-aminoquinoline) and over the 0.5 to 1% range for the other analytes. The method was applied to tablet samples stressed at high relative humidity and temperature. The relative standard deviation of the assay for the 6-aminoquinoline was less than 2% and less than 13% for the minor components. Calculated mass balances (sum of adinazolam plus degradation products in the degraded tablet divided by the same sum in the undegraded tablet) were less than 100% and were dependent on the extent of degradation in the tablet. The average mass balance result obtained for samples that were an average of 9.5% degraded was 95.0 ± 1.5%. It is possible that the decrease in mass balance with increase in percent degradation may be explained by the formation of many components at trace levels due to degradation by various permutations of hydrolytic and oxidative reaction pathways.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1016219927912
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  • 2
    Electronic Resource
    Electronic Resource
    Evidence for the Lack of a Human Metabolic Isotope Effect of a Deuterium Analog of Fluphenazine (1995)
    Springer
    Pharmaceutical research 12 (1995), S. 1388-1390 
    Details
    ISSN: 1573-904X
    Keywords: fluphenazine ; stable isotope ; deuterium labeled ; mass spectrometry ; schizophrenics ; pharmacokinetics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1016298329188
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  • 3
    Electronic Resource
    Electronic Resource
    Organization, inheritance and expression of acetohydroxyacid synthase genes in the cotton allotetraploid Gossypium hirsutum (1995)
    Springer
    Plant molecular biology 28 (1995), S. 837-846 
    Details
    ISSN: 1573-5028
    Keywords: acetohydroxyacid synthase ; gene organization ; gene expression ; herbicide resistance ; cotton ; Gossypium hirsutum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The acetohydroxyacid synthase (AHAS) gene family of the cotton AD allotetraploid Gossypium hirsutum has been cloned and characterized. We have identified six different AHAS genes from an analysis of genomic clones and Southern blots of genomic DNA. Four of the six genes are organized as tandem pairs, in which the genes are separated by only 2–3 kb. Conservation of restriction fragment length polymorphisms between G. hirsutum and A-genome and D-genome-containing diploid cottons was sufficient to assign the single genes in clones A5 and A19 to the A and D subgenomes, respectively. Each diploid genome has one tandem pair, but in these cases we could not make specific subgenomic assignments. DNA and deduced amino acid sequences were determined for the A5 and A19 genes, and an AHAS cDNA clone isolated from a leaflibrary. The sequence of the A19 gene matches that of the cDNA clone, while the A5 gene is 97.8% similar. The four genes comprising the tandem pairs are much less similar to the cDNA clone. The deduced amino acid sequences of the mature polypeptides encoded by the A5 and A19 genes are collinear with the housekeeping forms of AHAS from Arabidopsis thaliana, Nicotiana tabacum and Brassica napus. The constitutive expression of A5 and A19 was confirmed with RNase protection assays and northern blots. We conclude that these genes encode the main house-keeping froms of AHAS in G. hirsutum. Among the four AHAS genes comprising the two tandem pairs, at least two are functional. These genes exhibit either low-level constitutive expression (one or both of the ‘downstream’ genes of each pair), or highly specific expression in reproductive tissue (one or both of the ‘upstream’ genes of each pair). The AHAS gene family of G. hirsutum is more complex than that of other plants so far examined.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00042069
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  • 4
    Electronic Resource
    Electronic Resource
    Hexose transporters of tomato: molecular cloning, expression analysis and functional characterization (2000)
    Springer
    Plant molecular biology 44 (2000), S. 687-697 
    Details
    ISSN: 1573-5028
    Keywords: gene expression ; heterologous expression ; H+/hexose symporter ; Lycopersicon esculentum ; quantitative PCR ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A full-length (LeHT2) and two partial (LeHT1 and LeHT3) cDNA clones, encoding hexose transporters, were isolated from tomato (Lycopersicon esculentum) fruit and flower cDNA libraries. Southern blot analysis confirmed the presence of a gene family of hexose transporters in tomato consisting of at least three members. The full-length cDNA (LeHT2) encodes a protein of 523 amino acids, with a calculated molecular mass of 57.6 kDa. The predicted protein has 12 putative membrane-spanning domains and belongs to the Major Facilitator Superfamily of membrane carriers. The three clones encode polypeptides that are homologous to other plant monosaccharide transporters and contain conserved amino acid motifs characteristic of this superfamily. Expression of the three genes in different organs of tomato was investigated by quantitative PCR. LeHT1 and LeHT3 are expressed predominantly in sink tissues, with both genes showing highest expression in young fruit and root tips. LeHT2 is expressed at relatively high levels in source leaves and certain sink tissues such as flowers. LeHT2 was functionally expressed in a hexose transport-deficient mutant (RE700A) of Saccharomyces cerevisiae. LeHT2-dependent transport of glucose in RE700A exhibited properties consistent with the operation of an energy-coupled transporter and probably a H+/hexose symporter. The K m of the symporter for glucose is 45 μM.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026578506625
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  • 5
    Electronic Resource
    Electronic Resource
    Characterization and expression of Metallothionein-like genes in cotton (1996)
    Springer
    Plant molecular biology 31 (1996), S. 701-705 
    Details
    ISSN: 1573-5028
    Keywords: cotton ; gene expression ; Gossypium hirsutum ; metallothionein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have characterized cotton (Gossypium hirsutum L.) genes encoding type 1 metallothionein-like proteins that are highly expressed in roots. Little or no expression of these genes was detected in other organs and tissues. The deduced amino acid sequences have a high degree of similarity with type 1 metallothionein-like proteins from other plants, including a central hydrophobic domain flanked by conserved cysteine-rich motifs. The type 1 metallothionein-like genes of cotton are encoded by a small gene family. One gene (MT1-A) was analyzed in detail and found to have three exons which are 52, 83 and 397 bp long, and two introns 130 and 1042 bp in length. Three of the type 1 metallothionein-like genes are organized in a tandom array, and the 5′-flanking regions of these genes share a high degree of sequence similarity. Two of the clustered genes (MT1-A andMT1-B) are expressed at about equal levels in roots and use the same transcription start site. A 640 bp promoter fragment from theMT1-A gene was sufficient to direct expression of beta-glucuronidase (GUS) in transformed cotton roots. The expression was highest near the root tip.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00042243
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  • 6
    Electronic Resource
    Electronic Resource
    Characterization and expression of chitinase and 1,3-β-glucanase genes in cotton (1996)
    Springer
    Plant molecular biology 31 (1996), S. 911-916 
    Details
    ISSN: 1573-5028
    Keywords: chitinase ; cotton ; gene expression ; 1,3-β-glucanase ; Gossypium hirsutum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have isolated cDNA clones representing mRNAs encoding chitinase and 1,3-β-glucanase in cotton (Gossypium hirsutum L.) leaves. The chitinase clones were sequenced and found to encode a 28,806 Da protein with 71% amino acid sequence similarity to the SK2 chitinase from potato (Solanum tuberosum). The 1,3-β-glucanase clones encoded a 37,645 Da protein with 57.6% identity to a 1,3-β-glucanase from soybean (Glycine max). Northern blot analyses showed that chitinase mRNA is induced in plants treated with ethaphon or salicylic acid, whereas the levels of 1,3-β-glucanase mRNA are relatively unaffected. Southern blots of cotton genomic DNA and genomic clones indicated chitinase is encoded by a small gene family of which two members, Chi 2;1 and Chi 2;2, were characterized. These genes share 97% sequence identity in their transcribed regions. The genes were found to have three exons which are 309, 154 and 550 bp long, and two introns 99 and 154 bp in length. The 5′-flanking regions of Chi 2;1 and Chi 2;2 exhibit a large degree of similarity and may contain sequences important for gene response to chemical agents and fungal attack.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00019478
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  • 7
    Electronic Resource
    Electronic Resource
    Structure and expression of the maize gene encoding the phosphoenolpyruvate carboxylase isozyme involved in C4 photosynthesis (1989)
    Springer
    Plant molecular biology 12 (1989), S. 579-589 
    Details
    ISSN: 1573-5028
    Keywords: C4 photosynthesis ; gene structure ; gene expression ; genetic variation ; silent substitution ; Zea mays
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have determined the structure of the maize (Zea mays L. subsp.mays line B73) nuclear gene encoding the phosphoenolpyruvate (PEP) carboxylase isozyme involved in C4 photosynthesis. The gene is 5.3 kb long and has ten exons that range in size from 85 to 999 bp. The nine introns vary from 97 to 872 bp. The sequence of 663 bp of 5′-flanking and 205 bp of 3′-flanking DNA is reported along with the entire gene sequence. Several short repetitive sequences were found in the 5′-flanking DNA that have characteristics similar to elements important in the light regulation of pea genes encoding the small subunit of ribulose 1,5-bisphosphate carboxylase. In addition, some 5′-flanking sequence similarities were found in a comparison with other light-regulated genes from maize and wheat. The level of DNA sequence variation among different PEP carboxylase alleles is similar to the allelic variation observed for several other maize nuclear genes. The data suggest modern maize variaties have retained much of the genetic variation present in their ancestral forms. Finally, accumulation of transcripts encoding the PEP carboxylase isozyme involved in C4 photosynthesis is quite high in several structures besides leaves, including inner leaf sheaths, tassels and husks. This indicates that expression of this gene is not leaf-specific and may not necessarily be coupled to the development of Kranz anatomy.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00036971
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  • 8
    Electronic Resource
    Electronic Resource
    Characterization and expression of U1snRNA genes from potato (1992)
    Springer
    Plant molecular biology 19 (1992), S. 959-971 
    Details
    ISSN: 1573-5028
    Keywords: gene expression ; gene variants ; pre-mRNA splicing ; pseudogenes ; U1 small nuclear RNA
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract U1 small nuclear RNAs (U1snRNAs) occur in the nucleus of plants and animals where, complexed with several proteins in the form of U1 small nuclear ribonucleoprotein particles (U1snRNPs), they play an important role in precursor messenger RNA (pre-mRNA) splicing. Ten potato U1snRNA genes have been isolated on two genomic clones illustrating the clustering of this multigene family on the potato genome. Based on both the sequence of their coding regions and upstream regulatory elements, seven of the genes are potentially functional. The other three genes were pseudogenes with defective promoter or coding region sequences. Analysis of expression of individual cloned U1snRNA genes in transfected tobacco protoplasts was impossible due to the similarity of U1snRNA sequences in tobacco. However, by marking the coding regions with oligonucleotides or constructing chimaeric genes consisting of a potato U1snRNA promoter region and maize U5snRNA coding region, three of the U1 promoter regions were shown to be transcriptionally active.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00040528
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  • 9
    Electronic Resource
    Electronic Resource
    Structural analysis of bovine pancreatic thread protein (1990)
    Springer
    The protein journal 9 (1990), S. 623-632 
    Details
    ISSN: 1573-4943
    Keywords: Pancreatic thread protein ; primary structure ; mass spectrometry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Pancreatic thread protein (PTP) forms double helical threads in the neutralpH range after purification, undergoing freely reversible,pH-dependent globule-fibril transformation. The purified bovine PTP consists on SDS gels of two carbohydrate-free polypeptide chains (Grosset al., 1985). Plasma desorption mass spectrometry and amino acid sequence analysis now confirm that bovine PTP contains two disulfide-bonded polypeptides, an A chain of 101 amino acid residues with a molecular weight of 11,073 and a B chain of 35 residues with a molecular weight of 3970. The intact protein exhibits a molecular weight of 15,036, agreeing 〉99.9% with the molecular weight calculated from the sequence. The B chain sequence was determined by gas-phase Edman degradation of the intact polypeptide. The A chain sequence was determined from overlapping peptides generated by cleavage at lysyl, tryptophanyl, and aspartyl-prolyl residues. Based upon the bovine PTP cDNA structure, the two chains of the protein result from cleavage of a single polypeptide with removal of a dipeptide between the NH2-terminal A chain and COOH-terminal B chain. Comparison of bovine PTP with other proteins reveals significant structural relatedness with the single-chain homologues from human and rat pancreas and with the motif associated with Ca2+-dependent carbohydrate recognition domains. The physiological role of PTP has not yet been resolved. The protein is present in very high concentration in pancreatic secretion and it has been detected in brain lesions in Alzheimer's disease and Down syndrome and in regenerating rat pancreatic islets. The present results provide a firm protein base for ongoing molecular, physical-chemical, and structure-function studies of this unusual protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01025016
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  • 10
    Electronic Resource
    Electronic Resource
    Further Alkaloids Common to Ants and Frogs: Decahydroquinolines and a Quinolizidine (1999)
    Springer
    Journal of chemical ecology 25 (1999), S. 1179-1193 
    Details
    ISSN: 1573-1561
    Keywords: Alkaloids ; mass spectrometry ; infrared spectroscopy ; amphibians ; ants ; decahydroquinolines ; quinolizidines
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Three alkaloids—two minor decahydroquinolines (DHQs) and a major quinolizidine—were detected in an extract of a Brazilian myrmicine ant (Solenopsis (Diplorhoptrum) sp. picea group). One DHQ (3) was identical to a known frog-skin alkaloid, cis-195A (cis-5-methyl-2-propyldecahydroquinoline), while the second DHQ, an isomer of 3, designated 195J, was assigned a tentative cis-2-methyl-5-propyldecahydroquinoline structure (2) based on mass and infrared spectra. The third alkaloid proved identical to the frog-skin alkaloid 195C, for which a structure had not been previously proposed. Mass and infrared spectral analysis, including chemical ionization tandem mass spectrometry, indicated a 4-methyl-6-propylquinolizidine structure (1) for 195C. The four possible diastereomers were synthesized and the (6Z,10E)-4-methyl-6-propylquinolizidine diastereomer (1b) was identical to the natural alkaloid. Skin extracts of a population of a Madagascan mantelline frog contained, among other alkaloids, minor amounts of the same alkaloid triad 1–3 with 1 again predominating. The common occurrence of alkaloids 1–3 in both ant and frog supports the hypothesis that ants are a likely dietary source for sequestered frog-skin alkaloids and brings to six, the alkaloid classes common to ant and frog.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1020898229304
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