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  • 1
    Electronic Resource
    Electronic Resource
    Immunoassay and Activity of Calcium-Activated Neutral Proteinase (mCANP): Distribution in Soluble and Membrane-Associated Fractions in Human and Mouse Brain (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 58 (1992), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The millimolar form of calcium-activated neutral proteinase (mCANP) is generally regarded as a cytosolic enzyme in nonneuronal systems, although its subcellular localization in brain is less well established. To resolve conflicting reports on the localization of mCANP based on activity measurements, we developed an immunoassay for CANP and compared the content and activity of the molecule in soluble and membrane fractions of mouse and human brain. Western blot immunoassays, using two different antibodies specific for mCANP, demonstrated that mCANP content is 4.5 ng/g in human or mouse brain, about 0.0005% of the total protein. More than 95% of the total immunoreactive mCANP remained in the soluble fraction after 15,000 g centrifugation of the whole homogenate. mCANP activity was determined with [14C]azocasein as substrate after removing endogenous CANP inhibitor(s) by ion-exchange chromatography on DEAE-cellulose. Caseinolytic activity was detected only in fractions derived from the supernatant extract. The distribution of mCANP content and enzyme activity were unchanged when tissues were extracted with different concentrations of Triton X-100. These findings establish the usefulness and validity of the CANP immunoassay and demonstrate that mCANP in mouse and human brain is localized predominantly within the cytosol.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1992.tb11374.x
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  • 2
    Electronic Resource
    Electronic Resource
    Pollen-derived rice calli that have large deletions in plastid DNA do not require protein synthesis in plastids for growth (1992)
    Springer
    Molecular genetics and genomics 233 (1992), S. 145-150 
    Details
    ISSN: 1617-4623
    Keywords: Rice ; Albino ; Plastid DNA ; Linear DNA ; tRNAGlu
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Albino rice plants derived from pollen contain plastid genomes that have suffered large-scale deletions. From the roots of albino plants, we obtained several calli containing homogeneous plastid DNA differing in the size and position of the deletion. Southern blotting and pulsed field gel electrophoresis experiments revealed that the DNAs were linear molecules having a hairpin structure at both termini, existing as monomers (19 kb) or dimers, trimers and tetramers linked to form head-to-head and tail-to-tail multimers. This characteristic form is similar to that of the vaccinia virus, in which the replication origin is thought to lie at or near the hairpin termini. Furthermore, polymerase chain reaction experiments revealed complete loss of the ribosomal RNA genes of the plastid DNA. The results suggest that plant cells can grow without translation occurring in plastids. All of the deleted plastid DNAs commonly retained the region containing the tRNAGlu gene (trnE), which is essential for biosynthesis of porphyrin. As porphyrin is the precursor of heme for mitochondria and other organelles, it is considered thattrnE on the remnant plastid genome may be transcribed by an RNA polymerase encoded on nuclear DNA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00587572
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  • 3
    Electronic Resource
    Electronic Resource
    Specificity of calcium-activated neutral proteinase (CANP) inhibitors for human μCANP and mCANP (1993)
    Springer
    Neurochemical research 18 (1993), S. 231-233 
    Details
    ISSN: 1573-6903
    Keywords: Calcium-activated neutral proteinases ; calpains ; calpeptin ; leupeptin ; E64 ; human brain ; proteinase inhibitors
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We investigated the relative inhibition of purified human μCANP and mCANP by five cysteine proteinase inhibitors including N-acetyl-Leu-Leu-nor-leucinal (C-I) and N-acetyl-Leu-Leu-methioninal (C-II), calpeptin, E64, and leupeptin. Based on IC50 measurements, calpeptin and C-I were stronger inhibitors by one to two orders of magnitude than C-II, leupeptin or E64. None of the five inhibitors, however, exhibited greater specificity for human μCANP or mCANP. These results indicate that, although the inhibition of a given cellular event by these compounds may suggest CANP involvement, effects on μCANP cannot be discriminated from those on mCANP.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01474689
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