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  • Biochemistry and Biotechnology  (1)
  • Coleoptera  (1)
  • Organ-specific polypeptides  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    European archives of oto-rhino-laryngology and head & neck 226 (1980), S. 123-128 
    ISSN: 1434-4726
    Keywords: Organ of Corti ; Organ-specific polypeptides ; Two-dimensional polyacrylamide gel electrophoresis ; Guinea pig ; Rat ; Actin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Two polypeptides, OCP-I and OCP-II, specific to the organ of Corti of the guinea pig and the rat, were detected by two-dimensional polyacrylamide gel electrophoresis. They were neither present in other inner ear structures, nor in other organs tested. The two polypeptides constitute a substantial portion of the total protein of the organ of Corti. Both inner and outer layer of the organ of Corti contained approximately equal amounts of OCP-I and OCP-II. The molecular weights of OCP-I and OCP-II are 37,000 and 22,500 daltons, respectively. The corresponding pI values are 4.9 and 5.1, respectively. In addition, actin and tubulin were detected in both layers of the organ of Corti.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-1561
    Keywords: Dihydromatricaria acid ; triglyceride ; (Z)-dec-8-ene-4,6-diynoic acid ; glyceride ethers ; waxes ; antifeedant ; Chauliognathus lugubris ; Coleoptera ; Cantharidae ; accessory glands ; defense
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The soldier beetleChauliognathus lugubris is shown to contain triglycerides and glyceride ethers of 8-dihydromatricaria acid, and waxes of the C12 homolog, of this acid, as well as the previously reported free acid. The triglycerides contain one, two, or three dihydromatricariate moieties, with any remaining positions esterified with normal fatty acids. The glyceride ethers were monostearyl ethers of glycerol esterified with dihydromatricaria acid and oleic or linoleic acid. The waxes, which also include a dihydromatricaria chromophore in the alcohol moiety, occur only in the females and are present in paired accessory glands in the abdomen. The ethers are restricted to females and appear to be associated with developing eggs. The triglycerides are much more abundant in females than males. Triglycerides, glyceride ethers, and waxes represent about 95% of the dihydromatricariate moiety (average, ca. 590 μg) in females with free acid the remainder; in males free acid is present to over 50% (ca. 22 μg) and the remainder is triglyceride (ca. 15 μg). Larvae contain mainly tridihydromatricariate-substituted triglyceride and a smaller quantity of the free acid.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 46 (1995), S. 452-458 
    ISSN: 0006-3592
    Keywords: protein hydration ; enzymes in organic solvents ; adsorption isotherms ; essential water ; water activity ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A very sensitive NMR method has been developed for measuring deuterated water bound to proteins suspended in nonpolar solvents. This has been used to determine the amount of bound water as a function of water activity for subtilisin Carlsberg suspended in hexane, benzene, and toluene and for α-chymotrypsin in hexane. The adsorption isotherms for subtilisin in the three solvents are very similar showing that water activity can be usefully employed to predict the amount of water bound to proteins in nonpolar organic media. Comparison of the degree of enzyme hydration reached in nonpolar solvents with that obtained in air shows that adsorption of strongly bound water is hardly affected by the low dielectric medium, but adsorption of loosely bound water is significantly reduced. This suggests that the hydrophobic regions of the protein surface are preferentially solvated by solvent molecules, and that in a nonpolar environment formation of a complete monolayer of water over the protein surface is thermodynamically unfavorable. © 1995 John Wiley & Sons, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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