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  • 1
    Electronic Resource
    Electronic Resource
    Properties of enzymes that recognize modified structures in DNA (1984)
    Springer
    The protein journal 3 (1984), S. 73-85 
    Details
    ISSN: 1573-4943
    Keywords: Modification ; DNA glycosylases ; AP-endonucleases ; incision nucleases ; alkyl transferases
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The properties of the major classes of DNA repair enzymes, such as DNA glycosylases, AP-endonucleases, incision nucleases, and alkyl transferases, are reviewed. With the exceptions of the incision nucleases, the properties of the enzymes are quite similar in prokaryotic and eukaryotic cells. The incision nucleases probably do not recognize the modified base residues as such, but rather helical distortion brought about by the modifying agents. The other classes of enzymes are more or less specific for certain modified structures.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01024838
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  • 2
    Electronic Resource
    Electronic Resource
    Salmon Eggshell Protein Expression: A Marker for Environmental Estrogens (1999)
    Springer
    Marine biotechnology 1 (1999), S. 252-260 
    Details
    ISSN: 1436-2236
    Keywords: Key words: environmental estrogens, nonylphenol, estrogen, zona radiata, gene expression, salmon.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract: A liver complementary DNA expression library from Atlantic salmon (Salmo salar) pretreated with estradiol-17β (E2) was constructed and screened with antibodies raised against salmon eggshell (zona radiata) proteins. Two clones, SalZr2_19 and SalZr2_23 were sequenced and shown to encode proteins of approximately 50 kDa. SalZr2_23 contains 12 octamer sequence lpqr/kpa/vq repeats also found in SalZr2_19, but only twice. Alignment reveals that the two salmon sequences are similar to piscine zona radiata proteins and mammalian zona pellucida proteins. Several transcripts ranging from 2.3 to 12 kb appeared in liver extracts of E2-treated fish. Juvenile fish treated with E2 or 4-nonylphenol showed strong induction of zona radiata protein. The use of egg envelope transcriptional and translational induction in male or juvenile fish as a biological marker of environmental estrogens is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/PL00011774
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  • 3
    Electronic Resource
    Electronic Resource
    Cold adaption of enzymes: Structural comparison between salmon and bovine trypsins (1994)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 20 (1994), S. 149-166 
    Details
    ISSN: 0887-3585
    Keywords: crystal structure ; cold adaption ; catalytic efficiency ; protein stability ; anionic ; ectotherm ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The crystal structure of an anionic form of salmon trypsin has been determined at 1.82 Å resolution. We report the first structure of a trypsin from a phoikilothermic organism in a detailed comparison to mammalian trypsins in order to look for structural rationalizations for the cold-adaption features of salmon trypsin. This form of salmon trypsin (T II) comprises 222 residues, and is homologous to bovine trypsin (BT) in about 65% of the primary structure. The tertiary structures are similar, with an overall displacement in main chain atomic positions between salmon trypsin and various crystal structures of bovine trypsin of about 0.8 Å. Intramolecular hydrogen bonds and hydrophobic interactions are compared and discussed in order to estimate possible differences in molecular flexibility which might explain the higher catalytic efficiency and lower thermostability of salmon trypsin compared to bovine trypsin. No overall differences in intramolecular interactions are detected between the two structures, but there are differences in certain regions of the structures which may explain some of the observed differences in physical properties. The distribution of charged residues is different in the two trypsins, and the impact this might have on substrate affinity has been discussed. © 1994 Wiley-Liss, Inc.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340200205
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