C-terminal amino acid residue loss for deprotonated peptide ions containing glutamic acid, aspartic acid, or serine residues at theC-terminus

2006 ◽  
Vol 41 (7) ◽  
pp. 939-949 ◽  
Author(s):  
Zhong Li ◽  
Talat Yalcin ◽  
Carolyn J. Cassady
Keyword(s):  
Amino Acid ◽  
Glutamic Acid ◽  
Aspartic Acid ◽  
Amino Acid Residue ◽  
Peptide Ions ◽  
Terminal Amino Acid ◽  
Terminal Amino

scholarly journals Terminal Amino Groups in Wool and S-Carboxymethyl Kerateine 2

1957 ◽  
Vol 10 (2) ◽  
pp. 225 ◽  
Author(s):  
EOP Thompson
Keyword(s):  
Amino Acid ◽  
Glutamic Acid ◽  
Aspartic Acid ◽  
Amino Groups ◽  
Terminal Amino Acid ◽  
Total N ◽  
Purified Protein Derivative ◽  
Terminal Residue ◽  
Terminal Amino

The N-terminal residues of Merino 64's quality wool and of a purified protein derivative extracted from it, S-carboxymethyl kerateine 2, have been determined. A similar total N-terminal residue content is present in both wool and S�carboxymethyl kerateine 2 comprising glycine, serine, threoni~e, aspartic acid, glutamic acid, and alanine. These occur in different proportions in the two materials and valine is an additional N-terminal amino acid present only in wool.

scholarly journals Purification and Properties of Staphylocoagulase

1975 ◽  
Author(s):  
A.D. Muller ◽  
B. M. Bas ◽  
H. C. Hemker
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Aspartic Acid ◽  
Acid Composition ◽  
Isoelectric Point ◽  
Terminal Amino Acid ◽  
Purification And Properties ◽  
Terminal Amino

Staphylocoagulase, an exoprotein of coagulase positive staphylocoagulase, has been purified to a state in which only trace amounts of contaminating proteins are detectable.Purification was more than 35,000 fold, which is 7 times more than the highest value reported in the literature. The yield was about 15%.Aspartic acid was found as a single N-terminal amino acid in this preparation. The molecular weight is 61,000 and the isoelectric point lies at pH 4.53.The amino acid composition was determined.

scholarly journals Carbohydrate is linked through ethanolamine to the C-terminal amino acid of Trypanosoma brucei variant surface glycoprotein

1983 ◽  
Vol 209 (1) ◽  
pp. 261-262 ◽  
Author(s):  
A A Holder
Keyword(s):  
Amino Acid ◽  
Aspartic Acid ◽  
Trypanosoma Brucei ◽  
Carboxy Group ◽  
Surface Glycoprotein ◽  
Variant Surface Glycoprotein ◽  
Side Chain ◽  
Serine Residue ◽  
Terminal Amino Acid ◽  
Terminal Amino

The C-terminal amino acid of the variant surface glycoprotein from Trypanosoma brucei is glycosylated. For two variant proteins that terminate in an aspartic acid and a serine residue respectively, it was shown that the sugar side chain is linked through ethanolamine to the alpha-carboxy group of the amino acid.

Plasma Oxytocinase: The Synthesis and Biological Properties of the First Prodoct of the Degradation of Oxytocin by this Enzyme

1974 ◽  
Vol 52 (1) ◽  
pp. 60-66 ◽  
Author(s):  
B. M. Ferrier ◽  
J. M. Hendrie ◽  
L. A. Branda
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Pregnant Women ◽  
Amino Acid Residue ◽  
Biological Properties ◽  
Milk Ejection ◽  
Terminal Amino Acid ◽  
Molecular Features ◽  
Marked Inhibition ◽  
Terminal Amino

Oxytocin is hydrolytically cleaved in the presence of plasma oxytocinase to give an acyclic peptide, tyrosyl-isoleucyl-glutaminyl-asparaginyl-S-(S-cysteine)-cysteinyl-prolyl-leucyl-glycinamide (1,2-acyclic oxytocin). The synthesis of this peptide is described. It is shown to be of very low potency in milk-ejection-like activity and uterotonic activity. It does not inhibit the expression of these activities by oxytocin, suggesting that it does not interfere with the hormone's binding to target tissues. The presence of 1,2-acyclic oxytocin slightly inhibits the rate of degradation of oxytocin by plasma from pregnant women, in contrast to the marked inhibition of the degradation of cystine di-β-naphthylamide. The Km for the degradation of oxytocin is 30 times smaller than that of the degradation of cystine di-β-naphthylamide, which is of the same order as the Ki for the inhibition of the degradation of cystine di-β-naphthylamide by 1,2-acyclic oxytocin. These results, together with information on the substrate specificity of plasma oxytocinase with respect to the N-terminal amino acid residue, suggest that there are molecular features of oxytocin other than its N-terminal residue that facilitate its interaction with plasma oxytocinase.

The degradation of glycoproteins with lithium borohydride: Isolation and analysis ofO-glycopeptides with reducedC-terminal amino acid residue

2000 ◽  
Vol 26 (1) ◽  
pp. 45-53
Author(s):  
N. P. Arbatsky ◽  
L. M. Likhosherstov ◽  
M. V. Serebryakova ◽  
O. S. Brusov ◽  
V. N. Shibaev ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue ◽  
Terminal Amino Acid ◽  
Lithium Borohydride ◽  
Terminal Amino
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