Previous studies using lectin blotting suggested that histones in Artemia are glycosylated. A closer examination revealed that lectins nonspecifically bind histones, thus other methodologies were employed to study possible glycosylation of histones in Artemia. Pro-Q Emerald 300 fluorescent staining, which utilizes periodic acid oxidation of glycans, gave faint positive signals for all Artemia core histones. Putative Artemia histone H1 isolated from 12, 24, and 48 hours of development analyzed by LC/MS showed differential glycosylation and methylation. Glycan analysis by HPAEC-PAD revealed that at 12 hours of development putative histone H1 were modified by sugars, composed of glucose, fucose, N-acetylgalactosamine, N-acetylglucosamine, mannose, and galactose, at a mole ratio of 27 molecules for every molecule of protein, decreasing to less than one molecule of sugar for every molecule of protein by 24 and 48 hours of development. The differential glycosylation of various histone isoforms may be correlated with changes in transcription.
|Advisor:||Acey, Roger A.|
|Commitee:||Cohlberg, Jeffrey A., McAbee, Douglas D.|
|School:||California State University, Long Beach|
|Department:||Chemistry and Biochemistry|
|School Location:||United States -- California|
|Source:||MAI 51/05M(E), Masters Abstracts International|
|Subjects:||Molecular biology, Biochemistry, Developmental biology|
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