Polyalanylation of bovine somatotropin peptide 96–133
Publication type: Journal Article
Publication date: 1977-05-01
SJR: —
CiteScore: —
Impact factor: —
ISSN: 00052795
PubMed ID:
861255
Biochemistry, Genetics and Molecular Biology (miscellaneous)
Abstract
Polyalanylation of bovine somatotropin peptide 96-133 has been investigated. Polyalanylated peptides contained an average of 3-50 additional alanines per mole of peptide. As indicated by circular dichroism, the parent peptide and the polyalanylated peptides were helical at pH 4.0. The biological activity per mole of peptide with 50 additional alanies was approximately the same as that of the parent peptide.
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GOST
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Hara K., Sonenberg M. Polyalanylation of bovine somatotropin peptide 96–133 // Biochimica et Biophysica Acta (BBA) - Protein Structure. 1977. Vol. 492. No. 1. pp. 95-101.
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Hara K., Sonenberg M. Polyalanylation of bovine somatotropin peptide 96–133 // Biochimica et Biophysica Acta (BBA) - Protein Structure. 1977. Vol. 492. No. 1. pp. 95-101.
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RIS
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TY - JOUR
DO - 10.1016/0005-2795(77)90217-3
UR - https://doi.org/10.1016/0005-2795(77)90217-3
TI - Polyalanylation of bovine somatotropin peptide 96–133
T2 - Biochimica et Biophysica Acta (BBA) - Protein Structure
AU - Hara, Kenji
AU - Sonenberg, Martin
PY - 1977
DA - 1977/05/01
PB - Elsevier
SP - 95-101
IS - 1
VL - 492
PMID - 861255
SN - 0005-2795
ER -
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BibTex (up to 50 authors)
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@article{1977_Hara,
author = {Kenji Hara and Martin Sonenberg},
title = {Polyalanylation of bovine somatotropin peptide 96–133},
journal = {Biochimica et Biophysica Acta (BBA) - Protein Structure},
year = {1977},
volume = {492},
publisher = {Elsevier},
month = {may},
url = {https://doi.org/10.1016/0005-2795(77)90217-3},
number = {1},
pages = {95--101},
doi = {10.1016/0005-2795(77)90217-3}
}
Cite this
MLA
Copy
Hara, Kenji, and Martin Sonenberg. “Polyalanylation of bovine somatotropin peptide 96–133.” Biochimica et Biophysica Acta (BBA) - Protein Structure, vol. 492, no. 1, May. 1977, pp. 95-101. https://doi.org/10.1016/0005-2795(77)90217-3.