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  • 1985-1989  (4)
  • Biochemistry and Biotechnology  (3)
  • rod-cone interaction  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Cone function in congenital nyctalopia (1987)
    Springer
    Documenta ophthalmologica 65 (1987), S. 307-318 
    Details
    ISSN: 1573-2622
    Keywords: focal ERG ; nyctalopia ; oscillatory potentials ; rod-cone interaction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract A patient with congenital stationary night blindness (CSNB) (Schubert-Bornschein type) transmitted as an autosomal recessive trait was studied with several tests of electrical function as well as a variety of psychophysical procedures. Comparison of the patient's present findings with those obtained 23 years earlier showed that while rod thresholds have remained the same, cone sensitivity has decreased. Subjective flicker thresholds obtained following a bleach were unchanged during the course of dark adaptation. The absence of rod-cone interaction, together with an absent scotopic b-wave, implies that the defect is in the mid-retinal layers. Further, the absence of oscillatory potentials in the photopic electroretinogram (ERG) suggests that the interplexiform cell may be implicated in some manner. The focal ERG of the CSNB patient showed normal amplitude and normal phase delays, supporting the idea that the focal ERG samples primarily cone photoreceptor activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00149937
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Sequence simplification and the intra- and intermolecular self-recognition properties of vasopressin/neurophysin biosynthetic precursor (1989)
    Chicester [u.a.] : Wiley-Blackwell
    Journal of Molecular Recognition 1 (1989), S. 158-165 
    Details
    ISSN: 0952-3499
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The self-assembly properties of the arginine 8-vasopression/bovine neurophysin II (AVP/BNPII) biosynthetic precursor were studied using glycopeptide-deleted and sequence-redesigned semisynthetic derivaties. Semisythetic precursors were prepared by chemically coupling synthetic vasopressinyl sequence domains and native protein-derived neurophysin II domain. Measurement of precursor-protein association by extent of affinity chromatographic retardation on agarose-immobilizes BNPII verified that the semisynthetic precursor with native AVP sequence has an enhanced self-association propensity similar to that predicted for native precursor. Here, the stabilizing contacts between hormone and neurophysin domains, mainly the positively charged protonated α-amino group and tyrosyl 2 side chain of the hormone, are retained. Semisynthetic precusor variants in which the hormone domain is sequence-simplified by introducing alanyl residues in position not considered important for neurophysin recognition show non-reduced association to BNPII. In contrast, removal of one of the main contact element between hormone and neurophysin by acetylation of the hormone α-amino group abolishes potentiation of precursor self-association. The results show that the presence of the C-termial glycopeptide sequence domain of native vaspressin precursor is not required to promote self-assemblly of the precursor. The data verify the view proposed for the oxytocinyl precursor that intramolecular domain interaction is the triggering event which promotes the increase in affinity of precursor self-association (intermolecular self-recognition). The data also define some of the intramolecular self-recognition element in the folded precursor required for the high affinity intermolecular self-recognition.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jmr.300010403
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    A simple method for accurately locating and cutting strips from the isoelectric focusing gel during two-dimensional electrophoresis using the phastsystem (1989)
    Weinheim : Wiley-Blackwell
    Electrophoresis 10 (1989), S. 223-224 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A rapid and simple method has been developed for precisely locating and cutting 1-3 mm strips from the isoelectric focusing gel during two-dimensional electrophoresis using the PhastSystem. The protocol utilizes an easily constructed styrofoam template with marks to guide accurate cutting of the strips from the sample lanes. This system greatly enhances the reproducibility and quality of the two-dimensional patterns obtained.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150100313
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Ultrasensitive polychromatic silver staining of sodium dodecyl sulfate-polyacrylamide gels with the Gelcode system using the PhastSystem Development Unit (1989)
    Weinheim : Wiley-Blackwell
    Electrophoresis 10 (1989), S. 535-536 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The Gelcode color-based silver staining system, an improved formulation based on the original publication by Sammons et al. (Electrophoresis 1981, 2, 141-147) has been adapted to automated rapid staining in the PhastSystem Development Unit. The use of elevated temperatures in the fixation, washing, staining, and stabilization steps of the protocol reduces the total time of the process from 18 h to 1 h. The limit of detection, which is at least tenfold more sensitive than the silver staining protocol recommended for the PhastSystem, corresponds to 0.05-0.1 ng of protein per band. The method is applicable to both one- and two-dimensional polyacrylamide gels.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150100717
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    Paper (German National Licenses)
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