Determination of D- and L-amino acid residues in peptides. Use of tritiated hydrochloric acid to correct for racemization during acid hydrolysis

1970 ◽  
Vol 92 (25) ◽  
pp. 7449-7454 ◽  
Author(s):  
James M. Manning
Keyword(s):  
Amino Acid ◽  
Hydrochloric Acid ◽  
Acid Hydrolysis ◽  
Amino Acid Residues

Amino acid sequence of cyanogen bromide fragment CB5 of human hemopexin

1989 ◽  
Vol 54 (3) ◽  
pp. 803-810 ◽  
Author(s):  
Ivan Kluh ◽  
Ladislav Morávek ◽  
Manfred Pavlík
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Acid Hydrolysis ◽  
Cyanogen Bromide ◽  
Polypeptide Chain ◽  
Amino Acid Residues ◽  
Mild Acid Hydrolysis ◽  
Methionine Residue ◽  
Cyanogen Bromide Fragment ◽  
Mild Acid

Cyanogen bromide fragment CB5 represents the region of the polypeptide chain of hemopexin between the fourth and fifth methionine residue (residues 232-352). It contains 120 amino acid residues in the following sequence: Arg-Cys-Ser-Pro-His-Leu-Val-Leu-Ser-Ala-Leu-Thr-Ser-Asp-Asn-His-Gly-Ala-Thr-Tyr-Ala-Phe-Ser-Gly-Thr-His-Tyr-Trp-Arg-Leu-Asp-Thr-Ser-Arg-Asp-Gly-Trp-His-Ser-Trp-Pro-Ile-Ala-His-Gln-Trp-Pro-Gln-Gly-Pro-Ser-Ala-Val-Asp-Ala-Ala-Phe-Ser-Trp-Glu-Glu-Lys-Leu-Tyr-Leu-Val-Gln-Gly-Thr-Gln-Val-Tyr-Val-Phe-Leu-Thr-Lys-Gly-Gly-Tyr-Thr-Leu-Val-Ser-Gly-Tyr-Pro-Lys-Arg-Leu-Glu-Lys-Glu-Val-Gly-Thr-Pro-His-Gly-Ile-Ile-Leu-Asp-Ser-Val-Asp-Ala-Ala-Phe-Ile-Cys-Pro-Gly-Ser-Ser-Arg-Leu-His-Ile-Met. The sequence was derived from the data on peptides prepared by cleavage of fragment CB5 by mild acid hydrolysis, by trypsin and chymotrypsin.

Determination of Amino Acid Residues Responsible for Specific Interaction of Protein Kinases with Small Molecule Inhibitors

2018 ◽  
Vol 52 (3) ◽  
pp. 478-487 ◽  
Author(s):  
D. A. Karasev ◽  
A. V. Veselovsky ◽  
A. A. Lagunin ◽  
D. A. Filimonov ◽  
B. N. Sobolev
Keyword(s):  
Amino Acid ◽  
Protein Kinases ◽  
Small Molecule ◽  
Small Molecule Inhibitors ◽  
Specific Interaction ◽  
Amino Acid Residues

scholarly journals Establishment of a Two-Dimensional HPLC-MS/MS Method Combined with DCl/D2O Hydrolysis for the Determination of Trace Amounts of D-Amino Acid Residues in Proteins

2015 ◽  
Vol 36 (2) ◽  
pp. 45-50 ◽  
Author(s):  
Shoto ISHIGO ◽  
Eiichi NEGISHI ◽  
Yurika MIYOSHI ◽  
Hirohisa ONIGAHARA ◽  
Masashi MITA ◽  
...  
Keyword(s):  
Amino Acid ◽  
Two Dimensional ◽  
Amino Acid Residues

Evidence for Biosynthetical Equivalence of the Epimeric Isoleucine Residues in Angolide

1972 ◽  
Vol 50 (4) ◽  
pp. 428-439 ◽  
Author(s):  
R. O. Okotore ◽  
D. W. Russell
Keyword(s):  
Amino Acid ◽  
Physical Properties ◽  
Acid Hydrolysis ◽  
Column Chromatography ◽  
Mass Spectra ◽  
Mathematical Treatment ◽  
Amino Acid Residues ◽  
Analytical Results ◽  
Cyclic Intermediate

Pithomyces sacchari was grown on media containing L-valine. Instead of the metabolite angolide (cyclo-L-α-hydroxyisovaleryl1-erythro-L-isoleucyl2-L-α-hydroxyisovaleryl3-threo-D-isoleucyl4), synthesized on un-supplemented media, it produced a mixture with very similar physical properties. Acid hydrolysis liberated erythro-L- and threo-D-isoleucines (1:1), and DL-valine in amounts proportional to the exogenous valine concentration; L-α-hydroxyisovaleric acid was the only other component. Radioactivity from L-valine-U-14C was incorporated without dilution into valine, and with extensive dilution into the hydroxy acid.Partial fractionation of the mixture was achieved by column chromatography. Mass spectra of two fractions, containing different proportions of valine, were compared with the spectrum of angolide. A simple mathematical treatment showed that the fractions contained angolide, its divaline homologue, and a homologue with only one isoleucine replaced by valine. This must be a 1: 1 mixture of the two possible isomers, since any deviation from this ratio is inconsistent with the analytical results. It follows that the erythro-L- and the threo-D-isoleucine residues of angolide are equivalent with respect to their replacement by valine. It is inferred that angolide biosynthesis involves a cyclic intermediate containing both amino acid residues in the L configuration.

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