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  • 1
    Electronic Resource
    Electronic Resource
    Tissue-specific regulation of metallothionein and metallothionein mRNA accumulation in the Antarctic notothenioid, Notothenia coriiceps (2000)
    Springer
    Polar biology 23 (2000), S. 17-23 
    Details
    ISSN: 1432-2056
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The distribution of metallothionein and metallothionein mRNA was examined in brain, liver and kidney of the red-blooded Antarctic fish Notothenia coriiceps. Basal levels of metallothionein were detected by silver saturation assay; the analysis showed large differences in the metallothionein content, with an increasing amount in kidney, liver and brain, respectively. Reverse transcriptase-mediated polymerase chain reaction was used to amplify two distinct metallothionein cDNA species from RNA extracted from the three tissues examined. Northern blot analysis revealed a high constitutive expression of metallothionein mRNA in kidney, in spite of the low metallothionein content found in this tissue. The analysis of the distribution of the two metallothionein transcripts, termed MT-1 and MT-2, in the tissues showed that the MT-2 transcript was the major form of the metallothionein mRNA in kidney and brain, whilst in liver the expression levels of the two metallothionein transcripts were comparable. This tissue-specific expression of isometallothioneins in the Antarctic fish suggests the presence of an organ-specific regulation of the metallothionein genes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s003000050003
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  • 2
    Electronic Resource
    Electronic Resource
    The primary structure of papaya mosaic virus coat protein: A revision (1989)
    Springer
    The protein journal 8 (1989), S. 795-805 
    Details
    ISSN: 1573-4943
    Keywords: PMV-coat protein ; FAB mass spectrometry ; N-acetyl blocking group ; RP-HPLC
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The presence of an acetyl blocking group at theN-terminus of the coat protein of papaya mosaic virus has been identified by FAB mass spectrometry. Furthermore, we have found that theN-terminal sequence of the protein is four amino-acid residues (AC-Ser-Lys-Ser-Ser-) longer than that previously reported, while Glu instead of Gln is theC-terminal residue. The present paper shows that PMV-protein is made up of 215 amino acid residues, with a molecular mass of 22,960 Da.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01024903
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    Paper (German National Licenses)
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