Site-Specific PEGylation for High-Yield Preparation of Lys21-Amine PEGylated Growth Hormone-Releasing Factor (GRF) (1−29) using a GRF(1−29) Derivative FMOC-Protected at Tyr1and Lys12

2007 ◽  
Vol 18 (2) ◽  
pp. 500-506 ◽  
Author(s):  
Yu Seok Youn ◽  
Kang Choon Lee
Keyword(s):  
Growth Hormone ◽  
High Yield ◽  
Site Specific ◽  
Growth Hormone Releasing Factor

Growth hormone releasing factor (GRF) infusion in patients with active acromegaly

1985 ◽  
Vol 110 (1_Suppla) ◽  
pp. S144-S145
Author(s):  
M. LOSA ◽  
J. SCHOPOHL ◽  
P. G. CHIODINI ◽  
A. LIUZZI ◽  
K. VON WERDER
Keyword(s):  
Growth Hormone ◽  
Growth Hormone Releasing Factor ◽  
Active Acromegaly

Synthetic pancreatic growth hormone-releasing factor (GRF-40) stimulates the secretion of the endocrine pancreas

Diabetes ◽  
1986 ◽  
Vol 35 (1) ◽  
pp. 119-123 ◽  
Author(s):  
K. Hermansen ◽  
A. M. Kappelgaard ◽  
J. Esmann ◽  
H. Orskov
Keyword(s):  
Growth Hormone ◽  
Endocrine Pancreas ◽  
Growth Hormone Releasing Factor ◽  
Pancreatic Growth

Systematic Engineering of a Protein Nanocage for High-Yield, Site-Specific Modification

2018 ◽  
Author(s):  
Daniel D. Brauer ◽  
Emily C. Hartman ◽  
Daniel L.V. Bader ◽  
Zoe N. Merz ◽  
Danielle Tullman-Ercek ◽  
...  
Keyword(s):  
Small Molecules ◽  
Protein Modification ◽  
Positive Charge ◽  
Specific Protein ◽  
High Yield ◽  
Site Specific ◽  
Protein Cage ◽  
Protein Carriers ◽  
Site Selective ◽  
Targeted Library

<div> <p>Site-specific protein modification is a widely-used strategy to attach drugs, imaging agents, or other useful small molecules to protein carriers. N-terminal modification is particularly useful as a high-yielding, site-selective modification strategy that can be compatible with a wide array of proteins. However, this modification strategy is incompatible with proteins with buried or sterically-hindered N termini, such as virus-like particles like the well-studied MS2 bacteriophage coat protein. To assess VLPs with improved compatibility with these techniques, we generated a targeted library based on the MS2-derived protein cage with N-terminal proline residues followed by three variable positions. We subjected the library to assembly, heat, and chemical selections, and we identified variants that were modified in high yield with no reduction in thermostability. Positive charge adjacent to the native N terminus is surprisingly beneficial for successful extension, and over 50% of the highest performing variants contained positive charge at this position. Taken together, these studies described nonintuitive design rules governing N-terminal extensions and identified successful extensions with high modification potential.</p> </div>

scholarly journals Site-specific N-glycosylation analysis of animal cell culture-derived Zika virus proteins

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Alexander Pralow ◽  
Alexander Nikolay ◽  
Arnaud Leon ◽  
Yvonne Genzel ◽  
Erdmann Rapp ◽  
...  
Keyword(s):  
Zika Virus ◽  
Animal Cell ◽  
Gradient Centrifugation ◽  
Viral Envelope ◽  
Protein Glycosylation ◽  
High Yield ◽  
Structural Protein ◽  
Site Specific ◽  
E Protein ◽  
The Impact

AbstractHere, we present for the first time, a site-specific N-glycosylation analysis of proteins from a Brazilian Zika virus (ZIKV) strain. The virus was propagated with high yield in an embryo-derived stem cell line (EB66, Valneva SE), and concentrated by g-force step-gradient centrifugation. Subsequently, the sample was proteolytically digested with different enzymes, measured via a LC–MS/MS-based workflow, and analyzed in a semi-automated way using the in-house developed glyXtoolMS software. The viral non-structural protein 1 (NS1) was glycosylated exclusively with high-mannose structures on both potential N-glycosylation sites. In case of the viral envelope (E) protein, no specific N-glycans could be identified with this method. Nevertheless, N-glycosylation could be proved by enzymatic de-N-glycosylation with PNGase F, resulting in a strong MS-signal of the former glycopeptide with deamidated asparagine at the potential N-glycosylation site N444. This confirmed that this site of the ZIKV E protein is highly N-glycosylated but with very high micro-heterogeneity. Our study clearly demonstrates the progress made towards site-specific N-glycosylation analysis of viral proteins, i.e. for Brazilian ZIKV. It allows to better characterize viral isolates, and to monitor glycosylation of major antigens. The method established can be applied for detailed studies regarding the impact of protein glycosylation on antigenicity and human pathogenicity of many viruses including influenza virus, HIV and corona virus.

Effects on Feeding Behavior of Rats of a Cryptic Peptide from the C-Terminal End of Prepro-Growth Hormone-Releasing Factor*

Endocrinology ◽  
1987 ◽  
Vol 121 (6) ◽  
pp. 1960-1965 ◽  
Author(s):  
K. ARASE ◽  
T. SAKAGUCHI ◽  
M. TAKAHASHI ◽  
G. A. BRAY ◽  
N. LING
Keyword(s):  
Growth Hormone ◽  
Feeding Behavior ◽  
Growth Hormone Releasing Factor ◽  
Cryptic Peptide ◽  
Behavior Of Rats

scholarly journals Studies on peptides. CXXXVII Conventional solution synthesis of porcine hypothalamic growth hormone releasing factor (pGRF).

1986 ◽  
Vol 34 (4) ◽  
pp. 1814-1820 ◽  
Author(s):  
MASANORI SHIMOKURA ◽  
YOSHIAKI KISO ◽  
AKIHIKO NAGATA ◽  
MASABUMI TSUDA ◽  
HITOSHI SEKI ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Solution Synthesis ◽  
Growth Hormone Releasing Factor ◽  
Conventional Solution

Effect of Growth Hormone-Releasing Factor on Plasma Growth Hormone, Prolactin and Somatomedin C in Hypopituitary and Short Normal Children

1985 ◽  
Vol 22 (1-2) ◽  
pp. 32-45 ◽  
Author(s):  
Guy Van Vliet ◽  
Dani&egrave;le Bosson ◽  
Claude Robyn ◽  
Margareta Craen ◽  
Paul Malvaux ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Plasma Growth Hormone ◽  
Normal Children ◽  
Somatomedin C ◽  
Growth Hormone Releasing Factor
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