Amino acid composition and the amino terminal end groups of the α- and β-chains of four Lemur hemoglobins

1965 ◽  
Vol 109 (3) ◽  
pp. 571-578 ◽  
Author(s):  
Ralph A. Bradshaw ◽  
Larry A. Rogers ◽  
Robert L. Hill ◽  
John Buettner-Janusch
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Amino Terminal ◽  
End Groups

scholarly journals Localization and Characterization of the Cleavage-Associated Neoantigen in the Edomain of Fibrinogen

1977 ◽  
Author(s):  
E. F. Plow ◽  
T. S. Edgington
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Conformational Changes ◽  
Deae Cellulose ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Amino Terminal ◽  
Exclusion Chromatography

Plasmic cleavage of fibrinogen to generate fragment X partially exposes a specific cryptic molecular site, fg-Eneo. This site in the E domain of the molecule is further exposed during subsequent cleavage. We now report on localization of this site which provides an incisive marker for the structural and conformational changes associated with plasmic cleavage of fibrinogen. Fg-Eneo was stable to reduction and alkylation and the chains of the E fragment were separated by ion exchange chromatography on DEAE-cellulose. An active component was obtained and subjected to molecular exclusion chromatography on Sephadex G-50 to insure removal of intact fg-E. A fg-Eneo positive chain was recovered and identified as Eγ with respect to amino-terminal tyrosine, amino acid composition, and immunochemical analysis. The fg-Eneo site was stable to tryptic degradation, and tryptic peptides were prepared and separated by multiple molecular exclusion chromatographic steps. Final separation of two peptides of similar size was achieved on the basis of carbohydrate content by affinity chromatography on Concanavalin A. Only the active peptide was bound by the lectin. Purity and identification of the active tryptic peptide as γ36–53 was established by amino acid composition and sequence. These results establish that this region of the γ chain of fibrinogen is not present at the hydrated surface of the native molecule but that, in association with plasmic cleavage and conformational changes, this site is progressively exposed and provides a dynamic marker of the cleavage sequence.

The structure of apoferritin: Amino acid composition and end-groups

1962 ◽  
Vol 4 (4) ◽  
pp. 251-256 ◽  
Author(s):  
Pauline M. Harrison ◽  
T. Hofmann ◽  
W.I.P. Mainwaring
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
End Groups

scholarly journals Scrambled Prion Domains Form Prions and Amyloid

2004 ◽  
Vol 24 (16) ◽  
pp. 7206-7213 ◽  
Author(s):  
Eric D. Ross ◽  
Ulrich Baxa ◽  
Reed B. Wickner
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Sequence Composition ◽  
Amino Terminal ◽  
Rich Domain ◽  
The Many ◽  
Necessary And Sufficient

ABSTRACT The [URE3] prion of Saccharomyces cerevisiae is a self-propagating amyloid form of Ure2p. The amino-terminal prion domain of Ure2p is necessary and sufficient for prion formation and has a high glutamine (Q) and asparagine (N) content. Such Q/N-rich domains are found in two other yeast prion proteins, Sup35p and Rnq1p, although none of the many other yeast Q/N-rich domain proteins have yet been found to be prions. To examine the role of amino acid sequence composition in prion formation, we used Ure2p as a model system and generated five Ure2p variants in which the order of the amino acids in the prion domain was randomly shuffled while keeping the amino acid composition and C-terminal domain unchanged. Surprisingly, all five formed prions in vivo, with a range of frequencies and stabilities, and the prion domains of all five readily formed amyloid fibers in vitro. Although it is unclear whether other amyloid-forming proteins would be equally resistant to scrambling, this result demonstrates that [URE3] formation is driven primarily by amino acid composition, largely independent of primary sequence.

Phosphatidylinositol-specific phospholipase C FromBacillus cereus: Improved purification, amino acid composition, and amino-terminal sequence

1989 ◽  
Vol 39 (3) ◽  
pp. 315-325 ◽  
Author(s):  
Johannes J. Volwerk ◽  
Peter B. Wetherwax ◽  
Loreene M. Evans ◽  
Andreas Kuppe ◽  
O. Hayes Griffith
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Phospholipase C ◽  
Acid Composition ◽  
Terminal Sequence ◽  
Amino Terminal ◽  
Amino Terminal Sequence

Highly basic cyanogen bromide peptides from the proteins of turnip rosette virus and the Prunus strain of tomato bushy stunt virus

1986 ◽  
Vol 64 (12) ◽  
pp. 3043-3046
Author(s):  
J. H. Tremaine ◽  
W. P. Ronald
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Mosaic Virus ◽  
Acid Composition ◽  
Cyanogen Bromide ◽  
Sodium Dodecyl ◽  
Tomato Bushy Stunt Virus ◽  
Basic Peptide ◽  
Amino Terminal ◽  
Basic Peptides

The proteins of turnip rosette virus (TRosV) a sobemovirus, and the Prunus strain of tomato bushy stunt virus (TBSV-P) were cleaved with cyanogen bromide, and highly basic peptides were isolated by ion-exchange chromatography. The amino acid composition and sodium dodecyl sulphate – polyacrylamide gel electrophoresis indicated the basic peptide from TRosV had 40 amino acid residues, including 11 basic residues. This peptide had a composition similar to basic peptides isolated from the sobemoviruses, sowbane mosaic virus, and two strains of southern bean mosaic virus. The amino acid composition and size of the basic peptide from TBSV-P were similar to those found for the amino terminal sequence of the type strain of TBSV.

Structural homologies in alanine-rich acidic ribosomal proteins from procaryotes and eucaryotes

1979 ◽  
Vol 57 (6) ◽  
pp. 719-726 ◽  
Author(s):  
Louis Peter Visentin ◽  
Makoto Yaguchi ◽  
Alastair T. Matheson
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Sequence Homology ◽  
Ribosomal Proteins ◽  
Wheat Germ ◽  
Bacillus Stearothermophilus ◽  
Cell Types ◽  
Terminal Sequence ◽  
Amino Terminal

The amino acid composition and amino-terminal sequence have been determined for the alanine-rich, acidic ribosomal 'A' protein (equivalent to Escherichia coli L7/L12) from three procaryotic cell types that live under extreme environmental conditions (Arthrobacter glacialis, Clostridium pasteurianum, and Bacillus stearothermophilus) as well as from wheat germ, a eucaryote source. These data are compared with previously published 'A' protein sequences from other procaryotes and eucaryotes. All the procaryotic 'A' proteins, with the exception of the very acidic 'A' protein from Halobacterium cutirubrum, show similar charge, size, and amino acid composition, as well as an extensive sequence homology in the N-terminal region. Some differences are observed between gram-negative and gram-positive bacteria. The 'A' proteins from eucaryotes contain two tyrosine molecules, an amino acid absent in procaryotic 'A' proteins, as well as a reduced number of valine residues and an increased amount of aspartic acid. The N-terminal sequence of wheat germ 'A' protein shows considerable homology with other eucaryotic 'A' proteins and also with H. cutirubrum. It also shows some sequence homology with E. coli 'A' proteins.

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