Analyze Diet
FEBS letters1985; 185(1); 115-120; doi: 10.1016/0014-5793(85)80752-3

Mammalian ribonucleases. The absence of a glycosylated Asn-Pro-Thr sequence in horse ribonuclease and the presence of tryptophan at position 39 in horse and dromedary ribonuclease.

Abstract: Parts of the amino acid sequences of horse and dromedary pancreatic ribonuclease were reinvestigated. The sequence of residues 21-25 in horse ribonuclease is Ser-Asn-Pro-Thr-Tyr or Ser-Asn-Ser-Thr-Tyr. The asparagine in the latter sequence is glycosylated. Horse ribonuclease possesses four additional amino acid residues at the C-terminus, like a number of other ribonucleases. Position 39 in horse and dromedary ribonuclease is not deleted but is occupied by tryptophan.
Publication Date: 1985-06-03 PubMed ID: 3922790DOI: 10.1016/0014-5793(85)80752-3Google Scholar: Lookup
The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
  • Comparative Study
  • Journal Article

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research analyzes parts of the amino acid sequences of horse and dromedary pancreatic ribonuclease, discovering that horse ribonuclease does not contain a glycosylated Asn-Pro-Thr sequence and that both horse and dromedary ribonucleases have tryptophan at position 39.

Amino Acid Sequences Investigation

  • The study was focused on reevaluating parts of the amino acid sequences found in horse and dromedary pancreatic ribonuclease. The researchers specifically looked at the sequence of residues, which denotes the order of amino acids in a protein, ranging from 21 to 25 in horse ribonuclease.
  • It was found that the sequence in question is either Ser-Asn-Pro-Thr-Tyr or Ser-Asn-Ser-Thr-Tyr. In the latter sequence, the asparagine (Asn) is glycosylated, which means a sugar molecule is attached to it. However, the absence of a glycosylated Asn-Pro-Thr sequence was noted in horse ribonuclease.

Presence of Extra Amino Acid Residues and Tryptophan

  • The researchers also found that horse ribonuclease contains four additional amino acid residues at the C-terminus. The C-terminus is the end of an amino acid chain and the presence of additional residues there is also found in a number of other ribonucleases.
  • Another important discovery from the study is that the horse and dromedary ribonucleases have tryptophan at position 39. Tryptophan is an essential amino acid that the body cannot produce and must be obtained from the diet. Its presence was detected at the 39th position in the ribonuclease amino acid sequence of both the horse and dromedary.

Cite This Article

APA
Beintema JJ. (1985). Mammalian ribonucleases. The absence of a glycosylated Asn-Pro-Thr sequence in horse ribonuclease and the presence of tryptophan at position 39 in horse and dromedary ribonuclease. FEBS Lett, 185(1), 115-120. https://doi.org/10.1016/0014-5793(85)80752-3

Publication

ISSN: 0014-5793
NlmUniqueID: 0155157
Country: England
Language: English
Volume: 185
Issue: 1
Pages: 115-120

Researcher Affiliations

Beintema, J J

    MeSH Terms

    • Amino Acid Sequence
    • Animals
    • Asparagine
    • Camelus / metabolism
    • Carbohydrates / analysis
    • Chromatography, Gel
    • Cyanogen Bromide
    • Glycopeptides / analysis
    • Horses / metabolism
    • Pancreas / enzymology
    • Proline
    • Ribonucleases / analysis
    • Threonine
    • Tryptophan

    Citations

    This article has been cited 2 times.
    1. De Genst E, Silence K, Decanniere K, Conrath K, Loris R, Kinne J, Muyldermans S, Wyns L. Molecular basis for the preferential cleft recognition by dromedary heavy-chain antibodies. Proc Natl Acad Sci U S A 2006 Mar 21;103(12):4586-91.
      doi: 10.1073/pnas.0505379103pubmed: 16537393google scholar: lookup
    2. Beintema JJ, Blank A, Schieven GL, Dekker CA, Sorrentino S, Libonati M. Differences in glycosylation pattern of human secretory ribonucleases. Biochem J 1988 Oct 15;255(2):501-5.
      pubmed: 3202829