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  • 1
    Electronic Resource
    Electronic Resource
    Presence of non-fibrillar amyloid b protein in skin biopsies of Alzheimer's disease (AD), Down's syndrome and non-AD normal persons (1994)
    Springer
    Acta neuropathologica 88 (1994), S. 201-206 
    Details
    ISSN: 1432-0533
    Keywords: Key words Amyloid β protein ; Skin biopsy ; Alzheimer's disease ; Down's syndrome
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract A total of 66 skin biopsies from persons with Alzheimer's disease (AD) or Down's syndrome (DS) and from persons without AD were used in this study. The age range was from 7 to 89 years. Positive immunoreactivity of skin biopsies to monoclonal antibody 4G8, which is reactive to amino acid residue 17 – 24 of synthetic amyloid β protein (Aβ), and 4G8-Fab (the antigen-binding fragment of 4G8 IgG, reactive only to amyloid plaque) was observed in the epidermis-dermis junction or the basement membrane of the epidermis and in some blood vessels of the biopsy skins of 13/18 (72  %) AD, 9/10 (90  %) DS, and 14/38 (37  %) non-AD control cases. The Fisher exact probability test revealed a significant difference (P=0.0415 one-tailed) in immunoreactivity between AD and age-matched controls. There was also a significant difference (P=0.0152 one-tailed; P=0.0200 two-tailed) between DS and age-matched control in the same test. Immuno-gold electron microscopy examination of these cases with positive immunoreactivity revealed that the gold particles were deposited along the basement membrane of the epidermis. Amyloid fibrils were not observed in the regions with gold particles. Results of this study suggest that Aβ is associated with the basement membrane of skin and is present in amorphous, non-fibrillar form as soluble Aβ.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00293394
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  • 2
    Electronic Resource
    Electronic Resource
    Presence of non-fibrillar amyloid β protein in skin biopsies of Alzheimer's disease (AD), Down's syndrome and non-AD normal persons (1994)
    Springer
    Acta neuropathologica 88 (1994), S. 201-206 
    Details
    ISSN: 1432-0533
    Keywords: Amyloid β protein ; Skin biopsy Alzheimer's disease ; Down's syndrome
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract A total of 66 skin biopsies from persons with Alzheimer's disease (AD) or Down's syndrome (DS) and from persons without AD were used in this study. The age range was from 7 to 89 years. Positive immunoreactivity of skin biopsies to monoclonal antibody 4G8, which is reactive to amino acid residue 17–24 of synthetic amyloid β protein (Aβ), and 4G8-Fab (the antigen-binding fragment of 4G8 IgG, reactive only to amyloid plaque) was observed in the epidermis-dermis junction or the basement membrane of the epidermis and in some blood vessels of the biopsy skins of 13/18 (72%) AD, 9/10 (90%) DS, and 14/38 (37%) non-AD control cases. The Fisher exact probability test revealed a significant difference (P=0.0415 one-tailed) in immunoreactivity between AD and age-matched controls. There was also a significant difference (P=0.0152 one-tailed; P=0.0200 two-tailed) between DS and age-matched control in the same test. Immuno-gold electron microscopy examination of these cases with positive immunoreactivity revealed that the gold particles were deposited along the basement membrane of the epidermis. Amyloid fibrils were not observed in the regions with gold particles. Results of this study suggest that Aβ is associated with the basement membrane of skin and is present in amorphous, non-fibrillar form as soluble Aβ.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00293394
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  • 3
    Electronic Resource
    Electronic Resource
    Characterization of a glutathione S-transferase gene ATGST 1 in Arabidopsis thaliana (1998)
    Springer
    Plant cell reports 17 (1998), S. 700-704 
    Details
    ISSN: 1432-203X
    Keywords: Key wordsArabidopsis thaliana ; Environmental stress ; Glutathione S-transferase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A glutathione S-transferase (GST) gene was cloned in Arabidopsis thaliana. The gene, designated ATGST 1, contained the entire transcription unit in three exons interrupted by two introns. The combined sequence of three exons had an open reading frame which predicted a GST protein of 208 amino acids. Gene transcription has been reported to be induced by pathogen attack and dehydration. In the present study northern blot analysis using a gene-specific DNA probe in the 3′ untranslated region revealed that expression of the gene was also rapidly induced by other environmental stresses such as wounding, low temperature, high salt and DPE herbicide treatment. The promoter region of the gene contained the sequence motif ATTTCAAA that is known to be present in ethylene-responsive elements and other motifs that are highly conserved amongst stress-inducible gene promoters.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002990050468
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  • 4
    Electronic Resource
    Electronic Resource
    Molecular characterization and expression of a cDNA encoding copper/zinc superoxide dismutase from cultured cells of cassava (Manihot esculenta Crantz) (1999)
    Springer
    Molecular genetics and genomics 262 (1999), S. 807-814 
    Details
    ISSN: 1617-4623
    Keywords: Key words Cassava (Manihot esculenta) ; Chemical stress ; Environmental stress ; Oxidative stress ; Superoxide dismutase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A cDNA, mSOD1, encoding cytosolic copper/zinc superoxide dismutase (CuZnSOD) was cloned and characterized from cell cultures of cassava (Manihot esculenta Crantz) which produce a high yield of SOD. mSOD1 encodes a 152-amino acid polypeptide with a pI value of 5.84. Southern analysis using an mSOD1-specific probe indicated that a single copy of the mSOD1 gene is present in the cassava genome. The mSOD1 gene is highly expressed in cultured cells, as well as in intact stems and tuberous roots. It is expressed at a low level in leaves and petioles. Transcripts of mSOD1 were not detected in nontuberous roots. Transcriptional level of mSOD1 reaches a high level at stationary phase, and then sharply decreases during further culture. In excised cassava leaves, the mSOD1 gene responded to various stresses in different ways. The stresses tested included changes in temperature and exposure to stress-inducing chemicals. Levels of mSOD1 transcript increased dramatically a few hours after heat stress at 37° C and showed a synergistic effect with wounding stress. Levels decreased in response to chilling stress at 4° C and showed an antagonistic effect with wounding stress. The gene was induced by abscisic acid, ethephon, NaCl, sucrose, and methyl viologen. These results indicate that the mSOD1 gene is involved in the response to oxidative stress induced by environmental change.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/PL00013819
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  • 5
    Electronic Resource
    Electronic Resource
    Molecular characterization of cDNAs for two anionic peroxidases from suspension cultures of sweet potato (1999)
    Springer
    Molecular genetics and genomics 261 (1999), S. 941-947 
    Details
    ISSN: 1617-4623
    Keywords: Key words Peroxidase cDNAs ; Suspension cultures ; Environmental stress ; Sweet potato (Ipomoea batatas)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Two cDNAs for anionic peroxidase (PODs), swpa2 and swpa3, were isolated from suspension cultures of sweet potato (Ipomoea batatas), and their expression was investigated with a view to understanding the physiological function of PODs in relation to environmental stresses. Swpa2 (whose putative mature protein product would have a pI value of 4.1) and swpa3 (4.3) encode polypeptides of 358 and 349 amino acids, respectively. The genes from which they were derived are predominantly expressed in cultured cells of sweet potato; transcripts of swpa2 were not detected in any tissues of the intact plant, and transcripts of swpa3 were detected at a low level only in the stem tissue. During cell culture, the expression patterns of the two genes differed; the level of swpa2 RNA progressively increased during cell growth, whereas that of swpa3 reached a maximum at the stationary phase and decreased on further culture. The two genes responded differently to stresses such as wounding or chilling of leaves. Swpa2 was strongly induced 48 h after wounding, but swpa3 was not affected by this treatment. The two genes were also highly expressed upon chilling (4° C), but expression was reduced by prior acclimation at 15° C. In addition, both genes were strongly induced immediately after treatment with ozone, and expression had decreased to the basal level 12 h after treatment. The response of these two genes to stresses such as aging, wounding, and chilling are different from those of the POD genes (swpa1 encoding an anionic product and swpn1 a neutral peroxidase) that we described previously. The responses of the two genes were also different from each other. These results suggest that the two new POD genes are involved in overcoming oxidative environmental stress, and each POD gene may be regulated by cell growth and environmental stress in different ways.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380051041
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  • 6
    Electronic Resource
    Electronic Resource
    Some factors determining protein aggregation during ultrafiltration (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 42 (1993), S. 260-265 
    Details
    ISSN: 0006-3592
    Keywords: fouling ; ultrafiltration ; protein aggregates ; field emission scanning electron microscopy (FESEM) ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The factors contributing to protein aggregation in albumin ultrafiltration were investigated as a function of operation conditions. The nature of protein deposits was examined by electron microscopy. Protein aggregation appears to occur as a result of rapid supersaturation of protein molecules and high solvent velocity (shear) in the concentrated layer near the membrane surface. The shear occurring in the solvent flow on the membrane surface probably unfolds protein molecules and thus promotes flocculation due to collision between particles. © 1993 John Wiley & Sons, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260420216
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  • 7
    Electronic Resource
    Electronic Resource
    Effect of membrane morphology and operation on protein deposition in ultrafiltration membranes (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 47 (1995), S. 174-180 
    Details
    ISSN: 0006-3592
    Keywords: ultrafiltration membranes ; protein fouling ; BET measurements ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Membrane morphology is compared to protein depostion under passive adsorption and ultrafiltration conditions. Solute resistance of protein deposits for membranes of varying roughness, structure, and permeability can vary dramatically with operating conditions. Using Brunauer-Emmett-Teller adsorption isotherm (BET), study of the internal area and accessibility of several uttrafiltration membranes to protein deposition allows better understanding of the fouling mechanisms and interpretation of adsorbed protein quantities. © 1995 John Wiley & Sons, Inc.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260470208
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  • 8
    Electronic Resource
    Electronic Resource
    Acid hydrolysis of sweet potato for ethanol production (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 27 (1985), S. 316-320 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Studies were conducted to establish optimal conditions for the acid hydrolysis of sweet potato for maximal ethanol yield. The starch contents of two sweet potato cultivars (Georgia Red and TG-4), based on fresh weight, were 21.1 ± 0.6% and 27.5 ± 1.6%, respectively. The results of acid hydrolysis experiments showed the following: (1) both hydrolysis rate and hydroxymethylfurfural (HMF) concentration were a function of HCL concentration, temperature, and time; (2) the reducing sugars were rapidly formed with elevated concentrations of HCl and temperature, but also destroyed quickly; and (3) HMF concentration increased significantly with the concentration of HCl, temperature, and hydrolysis time.Maximum reducing sugar value of 84.2 DE and 0.056% HMF (based on wet weight) was achieved after heating 8% SPS for 15 min in 1N HCl at 110°C. Degraded 8% SPS (1N HCl, 97°C for 20 min or 110°C for 10 min) was utilized as substrate for ethanol fermentation and 3.8% ethanol (v/v) was produced from 1400 mL fermented wort. This is equal to 41.6 g ethanol (200 proof) from 400 g of fresh sweet potato tuber (Georgia Red) or an ethanol yield potential of 431 gal of 200-proof ethanol/acre (from 500 bushel tubers/acre).
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260270316
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  • 9
    Electronic Resource
    Electronic Resource
    Acid hydrolysis of Jerusalem artichoke for ethanol fermentation (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 28 (1986), S. 138-141 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260280124
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