Amino acid racemization dating: Evidence of apparent reversal in aspartic acid racemization with time in shells of Ostrea

1986 ◽  
Vol 50 (6) ◽  
pp. 1159-1161 ◽  
Author(s):  
R.W.L Kimber ◽  
C.V Griffin ◽  
A.R Milnes
Keyword(s):  
Amino Acid ◽  
Aspartic Acid ◽  
Amino Acid Racemization ◽  
Aspartic Acid Racemization

scholarly journals Non-Concordance of Radiocarbon and Amino Acid Racemization Deduced Age Estimates on Human Bone

Radiocarbon ◽  
1983 ◽  
Vol 25 (2) ◽  
pp. 647-654 ◽  
Author(s):  
R E Taylor
Keyword(s):  
Amino Acid ◽  
Aspartic Acid ◽  
Human Bone ◽  
Amino Acid Racemization ◽  
Aspartic Acid Racemization ◽  
Order Of Magnitude ◽  
Direct Counting ◽  
Organic Fractions ◽  
Skeletal Samples ◽  
Age Estimates

Radiocarbon determinations, employing both decay and direct counting, were obtained on various organic fractions of four human skeletal samples previously assigned ages ranging from 28,000 to 70,000 years on the basis of their D/L aspartic acid racemization values. In all four cases, the 14C values require an order of magnitude reduction in age.

The Racemization Rate Constant for Protein-Bound Aspartic Acid in Woodrat Middens

1974 ◽  
Vol 4 (3) ◽  
pp. 340-345 ◽  
Author(s):  
Michael G. Petit
Keyword(s):  
Amino Acid ◽  
Aspartic Acid ◽  
Rate Constant ◽  
Isomeric Ratio ◽  
Acid Mixture ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Amino Acid Racemization ◽  
Crotalus Viridis ◽  
Protein Environment

The racemization rate constant for aspartic acid has been determined from the D/L isomeric ratio in four strata of radiocarbon dated woodrat midden in Arizona. Two different methods of stereospecifically deaminating L-aspartic acid prior to the assay are compared. It is found that pure L-amino acid oxidase pretreatment of the DL aspartic acid mixture requires one less step than treatment with crude, dialyzed venom (Crotalus viridis) but that the two methods give the same results. Application of the theory of amino acid racemization dating is discussed in the context of the steric properties ofthe protein environment in which the racemization actually occurs.

scholarly journals Evidence for Selection at thefusedLocus ofDrosophila virilis

Genetics ◽  
2000 ◽  
Vol 155 (4) ◽  
pp. 1701-1709 ◽  
Author(s):  
Jorge Vieira ◽  
Brian Charlesworth
Keyword(s):  
Amino Acid ◽  
Aspartic Acid ◽  
Kinase Domain ◽  
Drosophila Virilis ◽  
Serine Threonine Kinase ◽  
Threonine Kinase ◽  
Usual Equilibrium ◽  
Replacement Site ◽  
Fused Gene ◽  
Significant Linkage

AbstractThe genomic DNA sequence of a 2.4-kb region of the X-linked developmental gene fused was determined in 15 Drosophila virilis strains. One common replacement polymorphism is observed, where a negatively charged aspartic amino acid is replaced by the noncharged amino acid alanine. This replacement variant is located within the serine/threonine kinase domain of the fused gene and is present in ~50% of the sequences in our sample. Significant linkage disequilibrium is detected around this replacement site, although the fused gene is located in a region of the D. virilis X chromosome that seems to experience normal levels of recombination. In a 600-bp region around the replacement site, all eight alanine sequences are identical; of the six aspartic acid sequences, three are also identical. The occurrence of little or no variation within the aspartic acid and alanine haplotypes, coupled with the presence of several differences between them, is very unlikely under the usual equilibrium neutral model. Our results suggest that the fused alanine haplotypes have recently increased in frequency in the D. virilis population.

scholarly journals Transforming growth factor alpha: mutation of aspartic acid 47 and leucine 48 results in different biological activities.

1988 ◽  
Vol 8 (3) ◽  
pp. 1247-1252 ◽  
Author(s):  
E Lazar ◽  
S Watanabe ◽  
S Dalton ◽  
M B Sporn
Keyword(s):  
Amino Acids ◽  
Biological Activity ◽  
Amino Acid ◽  
Growth Factor ◽  
Aspartic Acid ◽  
Transforming Growth Factor ◽  
Biologically Active ◽  
Single Amino Acid ◽  
Transforming Growth Factor Alpha ◽  
Factor Alpha

To study the relationship between the primary structure of transforming growth factor alpha (TGF-alpha) and some of its functional properties (competition with epidermal growth factor (EGF) for binding to the EGF receptor and induction of anchorage-independent growth), we introduced single amino acid mutations into the sequence for the fully processed, 50-amino-acid human TGF-alpha. The wild-type and mutant proteins were expressed in a vector by using a yeast alpha mating pheromone promoter. Mutations of two amino acids that are conserved in the family of the EGF-like peptides and are located in the carboxy-terminal part of TGF-alpha resulted in different biological effects. When aspartic acid 47 was mutated to alanine or asparagine, biological activity was retained; in contrast, substitutions of this residue with serine or glutamic acid generated mutants with reduced binding and colony-forming capacities. When leucine 48 was mutated to alanine, a complete loss of binding and colony-forming abilities resulted; mutation of leucine 48 to isoleucine or methionine resulted in very low activities. Our data suggest that these two adjacent conserved amino acids in positions 47 and 48 play different roles in defining the structure and/or biological activity of TGF-alpha and that the carboxy terminus of TGF-alpha is involved in interactions with cellular TGF-alpha receptors. The side chain of leucine 48 appears to be crucial either indirectly in determining the biologically active conformation of TGF-alpha or directly in the molecular recognition of TGF-alpha by its receptor.

scholarly journals Characterization of Trypsin Inhibitor in Florunner Peanut Seeds (Arachis hypogaea L.)1

1988 ◽  
Vol 15 (2) ◽  
pp. 81-84 ◽  
Author(s):  
E. M. Ahmed ◽  
J. A. Applewhite
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Aspartic Acid ◽  
Arachis Hypogaea ◽  
Trypsin Inhibitor ◽  
Low Molecular Weight ◽  
Arachis Hypogaea L ◽  
Amino Acid Profiles ◽  
Low Levels

Abstract Florunner peanut seeds contained five trypsin isoinhibitors. Amino acid profiles of the trypsin inhibitors fraction showed high levels of aspartic acid, half-cystine and serine and low levels of histidine and tyrosine. The molecular weight of the inhibitor was 8.3 KDa. The presence of multiforms of this inhibitor, its low molecular weight and the high amount of half-cystine indicate that peanut trypsin inhibitor is of the Bowman-Birk type.

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