Bullfrog Ghrelin Is Modified by n-Octanoic Acid at Its Third Threonine Residue
نویسندگان
چکیده
منابع مشابه
Bullfrog ghrelin is modified by n-octanoic acid at its third threonine residue.
We have identified the amphibian ghrelin from the stomach of the bullfrog. We also examined growth hormone (GH)-releasing activity of this novel peptide in both the rat and bullfrog. The three forms of ghrelin identified, each comprised of 27 or 28 amino acids, possessed 29% sequence identity to the mammalian ghrelins. A unique threonine at amino acid position 3 (Thr(3)) in bullfrog ghrelin dif...
متن کاملDetermination of Ghrelin Structure in the Barfin Flounder (Verasper moseri) and Involvement of Ingested Fatty Acids in Ghrelin Acylation
Ghrelin is a peptide hormone that is acylated with a fatty acid, usually n-octanoic acid, at the third amino acid (aa) residue (usually a serine or threonine), and this acylation is known to be essential for ghrelin activity not only in mammals but also in non-mammals, such as fish. However, the modification mechanisms of ghrelin modification in fish are not known. In this study, we elucidated ...
متن کاملOn the N-methyl-L-threonine residue in stendomycin.
Sir: In a previous communication^ to this Jour nal, the isolation of N-methyl-L-threonine from acid hydrolysates of stendomycin2~4) was briefly mentioned. We wish to report here some experiments that led to the final assignment of the configuration for this amino acid with two centers of asymmetry. The specific rotation of the N-methyl amino acid from stendomycin was in good agreement with the ...
متن کاملC octanoic acid breath test
Although scintigraphy, a non-invasive procedure, is usually considered to be the reference technique for measuring gastric emptying in humans, several drawbacks limit its application in routine practice. Expensive equipment is required and access to a nuclear medicine department, and the use of radioactive isotopes (generally Tc and In) can produce low but significant irradiation. It is diYcult...
متن کاملThreonine 89 Is an Important Residue of Profilin-1 That Is Phosphorylatable by Protein Kinase A
OBJECTIVE Dynamic regulation of actin cytoskeleton is at the heart of all actin-based cellular events. In this study, we sought to identify novel post-translational modifications of Profilin-1 (Pfn1), an important regulator of actin polymerization in cells. METHODOLOGY We performed in vitro protein kinase assay followed by mass-spectrometry to identify Protein Kinase A (PKA) phosphorylation s...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2001
ISSN: 0021-9258
DOI: 10.1074/jbc.m105212200