1,721,121 research outputs found
Dipendenza dal pH e dalla presenza di ioni fosfato della cinetica di rilascio del CO dalla mioglobina di Nassa mutabilis
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Seasonal dependence of cadmium molecular effects on Mytilus galloprovincialis (Lamarck, 1819) protamine-like protein properties
No full textMussels have a seasonal reproduction and cadmium is a common stressor in estuarine and coastal environments. In previous studies, we have shown that exposure to subtoxic doses of cadmium produced alterations in the properties of winter Mytilus galloprovincialis sperm protamine-like (PL) proteins. In this study, it was analyzed the possibility that these cadmium effects may be seasonal. Winter and summer mussels were exposed to CdCl2 , and it was tested the PL-proteins for cadmium bioaccumulation, electrophoretic pattern, DNA binding, and potentiality to induce DNA oxidative damage. It was found that cadmium exposure did not produce the same effects on PL-proteins of summer mussels that were produced on PL-proteins of winter mussels, that is: cadmium bioaccumulation, alterations in the acetic acid-urea polyacrylamide gels (AU-PAGE) and sodium dodecyl sulfate-PAGE pattern, a reduced DNA binding affinity and the ability to induce DNA oxidative damage. PL-proteins from summer mussels, apart from not being affected by all the abovementioned effects of cadmium, also showed a very low DNA binding affinity, independent of cadmium exposure. This study reveals clock-associated seasonal responses to cadmium in M. galloprovincialis. Understanding the mechanisms through which environmental signals guide biological rhythms is fundamental to understanding the seasonal sensitivity of this bioindicator, to use M. galloprovincialis in appropriate seasonal periods
Il ciclo cellulare
No full textRevisione e aggiornamento della traduzione italiana sulla IV edizione inglese del capitolo numero 1
Relevance of the K/R ratio of protamines and sperm H1 histones in DNA binding:possibile functional role
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Evidences on arginine-lysine side chains interaction for the formation aggregational states of the H1 histone
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