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  • 1995-1999  (3)
  • Vector peptide  (2)
  • mitochondria  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 178 (1998), S. 87-94 
    ISSN: 1573-4919
    Keywords: myocyte ; nonmuscle cell ; myofibril ; mitochondria ; Arrhenius plot ; activation energy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The degree to which developmentally related alterations in cardiac creatine kinase (CK) activity reflect modification of CK isoenzyme gene expression remains uncertain. The present studies addressed this question by assessing multiple aspects of CK in rat heart during the perinatal to adult transition. In addition to whole tissue, isolated and purified muscle and nonmuscle cells were studied, as well as myofibrillar, mitochondrial, and cytosolic subcellular fractions. Whole homogenate CK enzyme specific activity nearly doubled during the weanling to adult developmental period. Muscle cell CK activity increased by a similar magnitude. Nonmuscle cell activity decreased. In the adult heart, both myofibrillar and mitochondrial CK activities were augmented versus the weanling heart. The cytoplasmic fraction activity held constant during development. Electrophoretic isoenzyme analyses of both weanling and adult cardiac muscle cells indicated the presence of mitochondrial CK and MM-CK isoforms. Weanling heart nonmuscle cells contained mitochondrial, MM, MB, and BB isoforms; however, BB isoform was not detected in the adult heart nonmuscle cells. Arrhenius plots provided information regarding heart muscle and nonmuscle cell alterations during development. CK activation energies were also determined for whole tissue, muscle/nonmuscle cells, myofibrils, mitochondria, and cytosol. Results demonstrate that heterogeneous muscle/nonmuscle cellular composition and differential myofibrillar/mitochondrial subcellular composition account for normal, developmentally related changes in heart CK enzyme activity. CK isoenzyme gene expression changes were not detected in cardiac muscle cells, and transition of CK-B to CK-M gene expression is limited to nonmuscle cells during normal, weanling to adult development in the rat heart.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    International journal of peptide research and therapeutics 4 (1997), S. 227-230 
    ISSN: 1573-3904
    Keywords: Cellular uptake ; Vector peptide ; Conformation ; Circular dichroism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract We describe the synthesis of an amphipathic vectorpeptide which is able to form complexes with nucleicacids. Based on circular dichroism investigations, the nature of thestructure obtained in water is questioned. Thepeptide adopts an α-helical structure in TFEand is partially in a β-sheet conformation inphosphate buffer at low peptide concentrations.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    International journal of peptide research and therapeutics 4 (1997), S. 227-230 
    ISSN: 1573-3904
    Keywords: Cellular uptake ; Vector peptide ; Conformation ; Circular dichroism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary We describe the synthesis of an amphipathic vector peptide which is able to form complexes with nucleic acids. Based on circular dichroism investigations, the nature of the structure obtained in water is questioned. The peptide adopts an α-helical structure in TFE and is partially in a β-sheet conformation in phosphate buffer at low peptide concentrations.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
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