Partial characterization of dinoflagellate chromosomal proteins
dc.contributor.author | Rizzo, P. J. | en_US |
dc.contributor.author | Nooden, L. D. | en_US |
dc.date.accessioned | 2006-04-07T16:46:40Z | |
dc.date.available | 2006-04-07T16:46:40Z | |
dc.date.issued | 1974-05-31 | en_US |
dc.identifier.citation | Rizzo, P. J., Nooden, L. D. (1974/05/31)."Partial characterization of dinoflagellate chromosomal proteins." Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis 349(3): 415-427. <http://hdl.handle.net/2027.42/22353> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B73G8-47TG1SH-4X/2/57b1d60220537b182abe7262fb70b1fb | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/22353 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=4407518&dopt=citation | en_US |
dc.description.abstract | Dinoflagellate chromosomal proteins were analyzed by acrylamide gel electrophoresis. The electrophoretic pattern of acid-insoluble chromosomal proteins from Gyrodinium cohnii in sodium dodecylsulfate gels is less heterogeneous than that of corn, and is characterized by a paucity of bands representing molecular weights below 43 000. Acrylamide gel electrophoresis of G. cohnii and Peridinium trochoideum acid-soluble chromosomal proteins in urea at pH 3.2 gives a banding pattern quite different than that of typical histones. Acid-soluble protein from chromatin prepared by the two different methods and from both organisms migrates as one predominant band with a mobility slightly less than that of Histone IV from corn. Its molecular weight, estimated by sodium dodecylsulfate gel electrophoresis, is about 16000. It is a basic protein (basic/acidic amino acids 1.3) but differs from most histones in that it contains both cysteine and aromatic amino acids and somewhat lower levels of basic amino acids (18 mole % compared with 22 to 30% for histones). In addition, the major acid-soluble component is present in chromatin from log-phase cells but absent in chromatin from stationary-phase cells. For these reasons, the major acid-soluble protein is probably not a histone. | en_US |
dc.format.extent | 1378282 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Partial characterization of dinoflagellate chromosomal proteins | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Materials Science and Engineering | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Botany, University of Michigan, Ann Arbor, Mich. 48104, U.S.A. | en_US |
dc.contributor.affiliationum | Department of Botany, University of Michigan, Ann Arbor, Mich. 48104, U.S.A. | en_US |
dc.identifier.pmid | 4407518 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/22353/1/0000799.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0005-2787(74)90127-0 | en_US |
dc.identifier.source | Biochimica et Biophysica Acta | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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