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Changes in histone glycosylation throughout Artemia development

Author: Simon Moon
Publisher: [Long Beach, California] : California State University, Long Beach, 2012.
Dissertation: M.S. California State University, Long Beach 2012
Series: California State University, Long Beach.; Master's thesis collection, Dept. of Chemistry and Biochemistry.
Edition/Format:   Thesis/dissertation : Thesis/dissertation   Computer File : English
Summary:
Abstract: 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  Read more...
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Details

Genre/Form: Academic theses
Material Type: Thesis/dissertation, Internet resource
Document Type: Book, Computer File, Internet Resource
All Authors / Contributors: Simon Moon
ISBN: 9781267977441 1267977442
OCLC Number: 1089838587
Description: 1 online resource (xii, 95 leaves) : illustrations, charts
Series Title: California State University, Long Beach.; Master's thesis collection, Dept. of Chemistry and Biochemistry.
Responsibility: by Simon Moon.

Abstract:

Abstract: 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.

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