A
Alan Przybyla
Researcher at University of Georgia
Publications - 38
Citations - 23034
Alan Przybyla is an academic researcher from University of Georgia. The author has contributed to research in topics: Hydrogenase & Peptide sequence. The author has an hindex of 26, co-authored 38 publications receiving 22984 citations. Previous affiliations of Alan Przybyla include University of California, San Francisco & University of Texas Southwestern Medical Center.
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Journal ArticleDOI
Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease.
TL;DR: In this article, the rat pancreas RNA was used as a source for the purification of alpha-amylase messenger ribonucleic acid (RBA) using 2-mercaptoethanol.
Book ChapterDOI
Isolation of RNA using guanidinium salts.
Journal ArticleDOI
Messenger RNA for myosin polypeptides: Isolation from single myogenic cell cultures
Richard C. Strohman,Paul S. Moss,Julie Micou-Eastwood,Dennis Spector,Alan Przybyla,Bruce M. Paterson +5 more
TL;DR: Messenger RNA which stimilates the synthesis of myosin heavy chain in a reticulocyte lysate has been isolated from single myogenic cell cultures, and an active fraction from sucrose gradients migrates as 26S on formamide-polyacrylamide gels.
Journal ArticleDOI
The three classes of hydrogenases from sulfate-reducing bacteria of the genus Desulfovibrio
G. Fauque,Harry D. Peck,José J. G. Moura,B.H. Huynh,Yves Berlier,Daniel V. DerVartanian,Miguel Teixeira,Alan Przybyla,Paul A. Lespinat,Isabel Moura,Jean LeGall +10 more
TL;DR: Three types of hydrogenases have been isolated from the sulfate-reducing bacteria of the genus Desulfovibrio and it is suggested that selenium is a ligand to nickel and suggest that the redox active nickel is ligated by at least two cysteinyl thiolate and one selenocysteine selenolate residues.
Journal ArticleDOI
Structure-function relationships among the nickel-containing hydrogenases.
TL;DR: It is proposed that nickel is ligated solely by amino acid residues of the large subunit and that the non-heme iron clusters are ligated by other cysteine-rich polypeptides encoded in the hydrogenase operons which are not necessarily homologous in either structure or function.