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  • 1
    Electronic Resource
    Electronic Resource
    Electrocatalysis of Nitric Oxide Reduction by Water-Soluble Cobalt Porphyrin. Spectral and Electrochemical Studies (1994)
    s.l. : American Chemical Society
    Inorganic chemistry 33 (1994), S. 5847-5854 
    Details
    ISSN: 1520-510X
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ic00103a037
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    The role of proteolytic enzymes in protein degradation during senescence of rice leaves (1984)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 62 (1984), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The role of proteolytic enzymes in protein degradation of detached and intact leaves of rice seedling (Oryza sativa L. cv. Taiching Native 1) during senescence and of mature leaves during reproductive development was investigated. The amount of soluble protein decreased by about 50% in 2, 4, and 15 days for detached, intact and mature leaves, respectively. Three proteolytic enzyme activities were monitored with pH optima of 4.5 for hemoglobin-digesting proteinase, 5.5 for carboxypeptidase and 8.0 for aminopeptidase. No azocoll-digesting proteinase activity could be detected in rice leaves. Dialysis did not alter the activities of any of the three proteolytic enzymes. Acid proteinase activity and aminopeptidase activity were highly unstable during storage of the enzyme extracts at 4°C. Proteolysis was stimulated by inclusion of meroaptoethanal either in the extraction medium or the assay medium.Acid proteinase, carboxypeptidase and aminopeptidase were all present in detached, intact and mature leaves throughout senescence. There seems to be a direct correlation between protein degradation and increases of acid proteinase and carboxypeptidase activity in seedling leaves (detached and intact) during senescence. In senescing (detached and intact) leaves of seedlings the acid proteinase activity developed first, while that of carboxypeptidase developed later. Acid proteinase and carboxypeptidase may play major roles in protein degradation of leaves from seedlings during senscence. During reproductive development, protein degradation was associated with decreases in the activities of acid proteinase, carboxypeptidase and aminopeptidase in mature leaves suggesting that the enzymes were less important for protein degradation in this system. Hence, the role of protelytic enzymes in protein degradation during senescence of rice leaves appears to depend largely on the leaf system used.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1984.tb00376.x
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  • 3
    Electronic Resource
    Electronic Resource
    Common occurrence of homologues of petunia glycine-rich protein-1 among plants (1996)
    Springer
    Plant molecular biology 31 (1996), S. 163-168 
    Details
    ISSN: 1573-5028
    Keywords: petunia ; glycine-rich protein ; monocot ; dicot
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The presence of specific glycine-rich proteins (GRP) related to petunia GRP1 (ptGRP1) was examined in three species of monocots (wheat, barley and maize) and five species of dicots (rape, turnip, soybean, crabapple and tomato). Protein blot analysis showed that anti-ptGRP1 antibody cross-reacted with a single different polypeptide in all species except maize. The molecular mass of these polypeptides ranged from 14 to 55 kDa. Tissue-print immunoblots of rape petioles and stems showed that the rape ptGRP1 homologue, like ptGRP1, is primarily located in the vascular tissue, and that its expression decreases with developmental age of the tissue. In barley, the ptGRP1 homologue is found in leaf vascular bundles, and may also be present in the surrounding bundle sheaths. Unlike the dicots examined, expression of the protein did not appear to decrease significantly with developmental age.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00020616
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    Paper (German National Licenses)
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