Characterization of a protein containing D-aspartic acid in aged mouse lens

Muraoka, Shiro; Fujii, Nobutaka; Tamanoi, Itsuro; Harada, Kaoru

doi:10.1016/0006-291x(87)90810-2

Cited by 13 publications

(4 citation statements)

References 6 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Differences in the ambient temperatures of crown and root could play a role, because the ambient temperature of the crown is lower than that of the root. In addition, 2 A measurable in vivo racemization of aspartic acid takes place not only in dentin but also in other human and animal tissues with metabolically stable proteins, such as tooth enamel, crystalline lens, the white matter of the brain and intervertebral discs (Fujii et al 1989;Garner and Spector 1978;Man et al 1983;Masters et al 1977Masters et al , 1978Muraoka et al 1987 (Tung et al 1985). Thus, the biochemical environment in the root and crown may differ and be responsible for different racemization rates in coronal and root dentin.…”

Section: Discussionmentioning

confidence: 94%

Postmortem estimation of age at death based on aspartic acid racemization in dentin: Its applicability for root dentin

1993

View full text Add to dashboard Cite

The extent of aspartic acid racemization in total dentin and in dentin protein fractions from the roots of third molars was determined. In several cases coronal dentin was also investigated. The results of other authors, according to which the racemization of aspartic acid in root dentin apparently proceeds differently than in coronal dentin, could be confirmed. Consequently, the data published so far on age determination based on the extent of aspartic acid racemization in coronal dentin and the "entire dentin of longitudinal sections" cannot be applied to root dentin. In total root dentin and the acid soluble protein of root dentin, a close relationship was observed between the extent of aspartic acid racemization and age. Accordingly, estimation of age at death based on aspartic acid racemization in dentin is also possible for root dentin, apparently with good results. This is important particularly in those cases where a large portion of the coronal dentin is absent, for instance following dental treatment. In the investigation of root dentin, regression equations specific for root dentin must be employed in the estimation of age at death. Corresponding equations for third molars were calculated.

show abstract

Section: Discussionmentioning

confidence: 94%

Postmortem estimation of age at death based on aspartic acid racemization in dentin: Its applicability for root dentin

1993

View full text Add to dashboard Cite

show abstract

“…The eye lens peptides, such as crystallins, contain D-Asp in mice (Muraoka et al, 1987), bovine (Groenen et al, 1990;Muraoka et al, 1991) and humans (Masters et al, 1977(Masters et al, , 1978Garner and Spector, 1978;Fujii et al, 1991Fujii et al, , 1994a. In humans, peptides of tooth enamel (Helfman and Bada, 1975) or dentine (Helfman and Bada, 1976) include D-Asp and the erythrocyte membrane (McFadden and Clarke, 1982;Clarke, 1983, 1984) includes methylated D-Asp.…”

Section: D-amino Acid-containing Peptides and Configuration Determinamentioning

confidence: 98%

“…The racemization ratios were also determined by GC. Amino acids were derivatized to N-trifluoroacetyl amino acid isopropyl esters and separated by GC on a chiral stationary phase (Muraoka et al, 1987Fujii et al, 1989Fujii et al, , 1991Fisher et al, 1991). The derivatization with chiral reagent to N-trifluoroacetyl L-prolyl amino acid methyl ester and the determination by GC was also reported (Man et al, 1983).…”

Section: D-amino Acid-containing Peptides and Configuration Determinamentioning

confidence: 99%

Amino acid sequence and D/L‐configuration determination methods for D‐amino acid‐containing peptides in living organisms

Iida

Santa

Toriba

et al. 2001

Biomedical Chromatography

View full text Add to dashboard Cite

D-amino acid-containing peptides with biological activities have been isolated from invertebrates and amphibians, and partial racemization of amino acid residues in mammalian peptides associated with aging and diseases have been discussed. Here, we review the amino acid configuration determination methods in these peptides and recent progress of simultaneous determination method for sequence and configuration of amino acid residues. The applicability of C-terminus sequence analysis and mass spectrometry to configuration determination of amino acids is also discussed.

show abstract

“…However, it is now well-known that both d - and l -amino acids exist in natural molecules. d -amino acid residues were first discovered in peptidoglycans within bacterial cell walls 7 – 9 and peptidic antibiotics 7 , followed by the discovery of d -amino acid residues in amphibians 10 , 11 , spiders 12 , marine sponges 13 , mollusks 14 , 15 , insects 16 , crustaceans 17 , mammals 18 , 19 , and humans 20 , 21 . Biologically active peptides containing d -amino acids including didemnin B 22 , palau’amide 23 , cyclotheonamides 24 , and halicylindramides 13 have been reported to have various therapeutic potentials.…”

Section: Introductionmentioning

confidence: 99%

Determination of sequence and absolute configuration of peptide amino acids by HPLC–MS/CD-based detection of liberated N-terminus phenylthiohydantoin amino acids

Hahn

Wang

Choi

et al. 2022

Sci Rep

View full text Add to dashboard Cite

We report a method for the simultaneous determination of the sequence and absolute configuration of peptide amino acids using a combination of Edman degradation and HPLC–MS/CD. Phenylthiohydantoin (PTH) derivatives of 20 pairs of standard d- and l-amino acids were synthesized by the Edman reaction. The CD spectra of the derivatives revealed that each pair of the PTH derivatives exhibited the absorption with opposite signs at around 270 nm. These standard PTH derivatives showed well-resolved resolution without interference from byproducts in the ion chromatogram and clear positive/negative CD absorptions when subjected on a reversed phase HPLC–MS system coupled with a CD-2095 HPLC detector. This method was applied for the detection of a synthetic pentapeptide and a natural depsipeptide (halicylindramide C). The sequence and configuration of the pentapeptide and up to eight residues of halicylindramide C were successfully analyzed by this method. The amino acid configuration of the pentapeptide was also determined successfully by subjecting its acid hydrolysates to the Edman reaction followed by HPLC–MS/CD.

show abstract

Characterization of a protein containing D-aspartic acid in aged mouse lens

Cited by 13 publications

References 6 publications

Postmortem estimation of age at death based on aspartic acid racemization in dentin: Its applicability for root dentin

Postmortem estimation of age at death based on aspartic acid racemization in dentin: Its applicability for root dentin

Amino acid sequence and D/L‐configuration determination methods for D‐amino acid‐containing peptides in living organisms

Determination of sequence and absolute configuration of peptide amino acids by HPLC–MS/CD-based detection of liberated N-terminus phenylthiohydantoin amino acids

Contact Info

Product

Resources

About