Cleavage of the peptide chain of the blood group substances at the hydroxy amino acid residues

1965 ◽  
Vol 14 (12) ◽  
pp. 2195-2195
Author(s):  
V. A. Derevitskaya ◽  
S. G. Kara-Murza ◽  
N. K. Kochetkov
Keyword(s):  
Amino Acid ◽  
Blood Group ◽  
Peptide Chain ◽  
Amino Acid Residues ◽  
Hydroxy Amino Acid ◽  
Hydroxy Amino ◽  
Blood Group Substances

Depsipeptides Communication 31. Synthesis of depsipeptides containing ?-hydroxy ?-amino acid residues

1965 ◽  
Vol 14 (11) ◽  
pp. 1954-1957
Author(s):  
G. A. Ravdel' ◽  
N. A. Krit ◽  
V. A. Oladkina ◽  
L. A. Shchukina ◽  
M. M. Shemyakin
Keyword(s):  
Amino Acid ◽  
Amino Acid Residues ◽  
Hydroxy Amino Acid ◽  
Hydroxy Amino

Identification and Characterization of O-Biotinylated Hydroxy Amino Acid Residues in Peptides

1994 ◽  
Vol 219 (2) ◽  
pp. 240-248 ◽  
Author(s):  
B.T. Miller ◽  
M.E. Rogers ◽  
J.S. Smith ◽  
A. Kurosky
Keyword(s):  
Amino Acid ◽  
Amino Acid Residues ◽  
Hydroxy Amino Acid ◽  
Hydroxy Amino ◽  
Identification And Characterization

4-alkoxycarbonyloxazoles as β-hydroxy-α-amino acid synthons: efficient stereoselective syntheses of 3-amino-2,3,6-trideoxyhexoses and a hydroxy amino acid moiety of Al-77-B

Tetrahedron ◽  
1990 ◽  
Vol 46 (13-14) ◽  
pp. 4823-4846 ◽  
Author(s):  
Yasumasa Hamada ◽  
Akiyoshi Kawai ◽  
Toshiaki Matsui ◽  
Osamu Hara ◽  
Takayuki Shioiri
Keyword(s):  
Amino Acid ◽  
Acid Moiety ◽  
Hydroxy Amino Acid ◽  
Hydroxy Amino ◽  
Amino Acid Moiety ◽  
Stereoselective Syntheses

Influence of Blood Group and Secretor Status on Carbohydrate Structures in Human Gastric Mucins: Implications for Peptic Ulcer

1995 ◽  
Vol 89 (4) ◽  
pp. 405-415 ◽  
Author(s):  
R. L. Sidebotham ◽  
J. H. Baron ◽  
J. Schrager ◽  
J. Spencer ◽  
J. R. Clamp ◽  
...  
Keyword(s):  
Peptic Ulcer ◽  
Amino Acid ◽  
Blood Group ◽  
Average Length ◽  
Amino Acid Residues ◽  
Secretor Status ◽  
Increased Risk ◽  
The Mean ◽  
The Difference ◽  
Carbohydrate Chains

1. The content and distribution of carbohydrate was examined in mucus glycopolypeptides from human antral mucosae. 2. The mean amount of carbohydrate per 1000 amino acid residues was found to be similar in glycopolypeptides with A, B or H activity. It was slightly, though significantly, less in glycopolypeptides lacking these determinants, because carbohydrate chains were of a shorter average length than in the A-, B- or H-active preparations. This difference was reflected in the sizes of oligosaccharide—alcohols released from representative glycopolypeptides with alkaline borohydride. 3. Differences between A-, B- or H-active and non-secretor glycopolypeptides in terms of the mean number of carbohydrate chains per 1000 amino acid residues were found to be small, and without significance. 4. The average number of peripheral monosaccharide units per 1000 amino acid residues was greater in A-active than in H-active, and least in non-secretor, glycopolypeptides. This order was reversed for monosaccharide units incorporated into skeletal (core plus backbone) structures. The difference in each case was statistically significant. 5. These findings suggest that the increased risk of peptic ulcer associated with blood group O and non-secretor status is unlikely to be attributable to an inherent deficiency in the protective mucus layer, linked to differences between mucins that are associated with A, B or H activity. Other hypotheses linked to infection with Helicobacter pylori are examined.

The C-terminal sequence of amino acid residues of κ-casein isolated from buffalo's milk

1967 ◽  
Vol 34 (1) ◽  
pp. 85-88 ◽  
Author(s):  
M. H. Abd El-Salam ◽  
W. Manson
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Peptide Chain ◽  
Amino Acid Residues ◽  
Terminal Sequence ◽  
Carboxypeptidase A ◽  
Phosphorous Content ◽  
Single Peptide

SummaryWhen κ-casein from buffalo's milk was treated with carboxypeptidase A (EC 3. 4. 2. 1),4 amino acids, valine, threonine, serine and alanine were released from the protein in a manner consistent with the view that they originate in the C-terminal sequence of a single peptide chain. The amounts produced suggest a minimum molecular weight for buffalo κ-casein of approximately 17000, in agreement with the value calculated from the phosphorous content on the basis of the presence of 2 phosphorus atoms/molecule. A comparison is made with the C-terminal sequence reported for bovine κ-casein.

scholarly journals Concise and Straightforward Asymmetric Synthesis of a Cyclic Natural Hydroxy-Amino Acid

Molecules ◽  
2014 ◽  
Vol 19 (12) ◽  
pp. 19516-19531 ◽  
Author(s):  
Mario Simirgiotis ◽  
Javier Vallejos ◽  
Carlos Areche ◽  
Beatriz Sepúlveda
Keyword(s):  
Amino Acid ◽  
Asymmetric Synthesis ◽  
Hydroxy Amino Acid ◽  
Hydroxy Amino

ON THE OXIDATION OF DIPEPTIDES CONTAINING HYDROXY-AMINO ACID RESIDUE BY PERIODIC ACID

1957 ◽  
Vol 44 (8) ◽  
pp. 471-476 ◽  
Author(s):  
SETURO FUJII ◽  
KIKUO ARAKAWA ◽  
NOBUHIKO AOYAGI
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue ◽  
Periodic Acid ◽  
Hydroxy Amino Acid ◽  
Hydroxy Amino

D-Threonine Aldolase and Its Application to D -β-Hydroxy-£-Amino Acid Synthesis

1992 ◽  
pp. 96-99
Author(s):  
Masahisa Ikemi ◽  
Tadashi Morikawa ◽  
Teruzo Miyoshi ◽  
Sakayu Shimizu ◽  
Michihiko Kataoka ◽  
...  
Keyword(s):  
Amino Acid ◽  
Acid Synthesis ◽  
Amino Acid Synthesis ◽  
Hydroxy Amino Acid ◽  
Threonine Aldolase ◽  
Hydroxy Amino

scholarly journals Anti-M monoclonal antibodies cross-reacting with variant Mg antigen: an example of modulation of antigenic properties of peptide by its glycosylation

Blood ◽  
1994 ◽  
Vol 84 (7) ◽  
pp. 2340-2345 ◽  
Author(s):  
E Jaskiewicz ◽  
M Czerwinski ◽  
D Syper ◽  
E Lisowska
Keyword(s):  
Monoclonal Antibodies ◽  
Amino Acid ◽  
Blood Group ◽  
Polypeptide Chain ◽  
Protein Glycosylation ◽  
Glycophorin A ◽  
Amino Acid Residues ◽  
Terminal Portion ◽  
Peptide Analogs ◽  
Antigenic Properties

Abstract Some monoclonal antibodies (MoAbs) directed against blood group M- related epitope of glycophorin A (GPA) were found to agglutinate rare variant erythrocytes carrying GPA of Mg type. In contradistinction to normal GPA-M or -N, the N-terminal portion of GPA-Mg is not glycosylated. Therefore, the multipin peptide synthesis was used for testing the specificity of the cross-reacting MoAbs. Among several anti- M and anti-N MoAbs tested, only three anti-M (E3, E6, 425/2B) agglutinated Mg erythrocytes and showed binding to the synthetic octapeptides corresponding to N-terminal sequences of GPA-M (SSTTGVAM), GPA-N (LSTTEVAM), and GPA-Mg (LSTNEVAM). Testing multiple peptide analogs (window and replacement analysis) showed that these MoAbs were specific for peptidic epitope in which Met8 and Val6 were the most essential amino acid residues. The amino acid replacements Ser<-->Leu1 or Gly<-->Glu5 (M v N) and Thr<-->Asn4 (M and N v Mg) had no or negligible effect on the reaction of synthetic peptides with the MoAbs. However, when Ser2, Thr3, and Thr4 carry O-linked sialooligosaccharides (normal GPA-M or -N), the MoAbs recognize Gly5- and sialic acid- dependent blood group M-related epitope. An interesting finding concerning anti-M/Mg MoAbs described here is the fact that glycosylation of amino acid residues adjacent to the most important part of peptidic epitope not only differentially modulates the proper exposure of peptidic epitope, but also alters the requirement for some amino acid residues present within the epitope. Pathologic conditions, including hematologic disorders, are often accompanied by alterations in protein glycosylation, resulting not only from differences in the structure of antigen polypeptide chain, but also from changes in specificity or expression of enzymes involved in glycosylation. Our present findings draw attention to possibility of the bidirectional modulation of protein antigenicity by glycosylation and may be helpful in interpretation of some results obtained with MoAb used for diagnostic or other purposes.

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