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  • Biochemistry and Biotechnology  (4)
  • diapause protein  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Utilization of normal alkanes by yeasts (1966)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 8 (1966), S. 549-565 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A stable mixed yeast culture designated as Culture 4, consisting of Candida intermedia and Candida lipolytica was investigated. The culture was judged stable based on uniformity of fermentation results and the nearly constant ratio of the two organisms at the completion of fermentations. However, the ratio of the two organisms at different times during the fermentation was not determined. The mixed culture grew more rapidly on n-alkanes than did C. intermedia; C. lipolytica did not grow on unsupplemented mineral salt-n-alkane medium. Solid n-alkanes were dissolved in 2,6,0,14-tetramethylpentadecane (pristane) for investigation as carbon sources. With Culture 4, on n-alkanes ranging from pentadecane (C15) through octacosane (C28), cell yields were 74.2-89.5%; generation times were 3.0-8.0 hr. during the exponential growth phase. The fastest growth rates and highest cell yields were obtained with docosane (C22) as substrate. The cells obtained contained 6.75-8.81% nitrogen and 1.9-13.4% lipid. Crude protein yields were 34.4-47.6%. The oxidation of n-alkanes by C. intermedia was studied manometrically with resting whole cells. The alkaneoxidizing system of this organism appears to be constitutive and nonspecific for alkane substrates.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260080408
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  • 2
    Electronic Resource
    Electronic Resource
    Growth of a yeast of normal alkanesSupported in part by grant AI 02967-05 from the National Institutes of Health. (1964)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 6 (1964), S. 299-307 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A soil isolate, HD-5, identified as closely resembling Candida intermedia, was grown on normal alkanes ranging from dodecane (C12) to octadecane (C18). The growth rate of the organism increased with increasing length of the alkane chain. The shortest generation time was 4.5 hr. with octadecane as the carbon source. Cell yields of 82% were common with even numbered alkanes from C14 through C18. The cell yields appeared to decrease with shorter chain (C12 or below) and odd-numbered chain alkanes. The cellular nitrogen ranged from 6.9 to 7.5% and the highest lipid content found was 10.3% (with C17).
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260060305
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  • 3
    Electronic Resource
    Electronic Resource
    Utilization of gas oil by a yeast culture (1966)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 8 (1966), S. 567-580 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A mixed yeast culture (Culture 4) was grown on representative gas oil samples as well as paraffin wax. Culture 4 was found to utilize n-paraffinic hydrocarbons almost quantitatively from most gas oil fractions; significant alteration of other hydrocarbon components was not detected. Generation times of 4.0-9.0hr. were typical during the exponential growth phase in fermentations with various gas oil fractions. Cell yields were 70-90% based on n-paraffin utilization. The culture appeared to exhibit maximum efficiency of n-alkane removal in the C19 to C24 range. The cells recovered from the fermentations contained 8.8-9.3% nitrogen. Paraffin wax also served as a suitable carbon source when dissolved in 2,6,10,14-tertramethylpentadecane (pristane). However, substrate utilization appeared to be incomplete.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260080409
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  • 4
    Electronic Resource
    Electronic Resource
    Novel poly-substituted aryl acridinium esters and their use in immunoassay (1989)
    New York : Wiley-Blackwell
    Journal of Bioluminescence and Chemiluminescence 4 (1989), S. 88-98 
    Details
    ISSN: 0884-3996
    Keywords: Immunoassay ; acridinium ester ; chemiluminescence ; liposomes ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A new series of stable acridinium ester conjugates have been developed for use as non-isotopic labels in immunoassay. They have proved to be a flexible alternative to radioimmunoassay. We present data showing the successful development of immunoassays in sandwich, competitive and receptor formats. In addition, hydrophilic acridinium ester analogues have been synthesized, encapsulated in liposomes, and utilized as labels in immunoassay. The potential of this technology is discussed.
    Additional Material: 13 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bio.1170040115
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  • 5
    Electronic Resource
    Electronic Resource
    A diapause associated protein of the pink bollworm Pectinophora gossypiella saunders (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 21 (1992), S. 1-11 
    Details
    ISSN: 0739-4462
    Keywords: hemolymph proteins ; diapause protein ; larval diapause ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A diapause associated protein was electrophoretically isolated from the hemolymph of diapausing last instar larvae of the pink bollworm Pectinophora gossypiella. This protein (Mr ∼490,000, glycolipoprotein) was given the name Pectinophora diapause protein (PDP). It is composed of one subunit (Mr 103,000). The concentration of PDP increased dramatically in the hemolymph of diapausing larvae from 17.4% in prediapause (PD) phase to 29.2% in early diapause (ED) phase reaching a level of 38.6% in larval hemolymph of middiapause (MD) phase. The concentrations of total proteins in the hemolymph of active feeding (A), PD, ED, and MD larvae were 69.8, 106.6, 113.3, and 118 mg/ml, respectively, while those in the fat body of the same larvae were 7.1, 7.4, 8.8, and 4.5 mg/g, respectively. In Pectinophora a drop in the concentration of fat body proteins coincided with a corresponding increase in hemolymph proteins, which suggests an active release of protein from the fat body into the hemolymph during the development of diapause. A partial amino acid sequence of pectinophorin showed the first 15 amino acids starting from the amino terminus of the peptide chain: N-ALA-LYS-THR-ILEU-VAL-GLU-ASN-MET-PRO-PRO-THR-PRO-LEU-ASN-ALA-C. © 1992 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940210102
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  • 6
    Electronic Resource
    Electronic Resource
    In vitro translation of diapause mRNA from the fat body of active and diapause larvae of the pink bollworm, Pectinophora gossypiella (Saunders) (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 23 (1993), S. 1-11 
    Details
    ISSN: 0739-4462
    Keywords: diapause protein ; poly(A)+ RNA ; larval diapause ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A diapause associated protein (DAP) (Mr 103,000) was isolated from the hemolymph and fat body of diapausing fourth instar larvae of the pink bollworm Pectinophora gossypiella. The protein has been named Pectinophora diapause protein (PDP). The in vitro translation peptide patterns of total RNA from the fat body of actively feeding fourth instar, wandering, prediapause, early diapause, mid-diapause, and late diapause larvae in rabbit reticulocyte lysates showed the presence of poly (A)+ RNA sequence of PDP. The antigen was immuno-precipitated by polyclonal antiserum. It was concluded that the transcription of the PDP gene in the fat body cells started in the late fourth instar larva and that the expression of this gene was regulated at the level of transcription in the fat body of diapausing larvae. Northern hybridization analysis revealed that wandering fourth instar larvae (diapause individuals) maintain a relatively low level of diapause message (mRNA/2.4 kb) in their fat body cells which may be necessary for the induction of diapause. © 1993 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940230103
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