Peptide histidine isoleucine

Seroogy K, Tsuruo Y, Hokfelt T, Walsh J, Fahrenkrug J, Emson PC, Goldstein M (1988) Further analysis of presence of peptides in dopamine neurons cholecystokinin, peptide histidine-isoleucine/vasoactive intestinal polypeptide and substance P in rat supramammillary region and mesencephalon. Exp Brain Res 72 523-534. 

However, in the cases examined so far, the molar solubility in DMF has not increased significantly. The 1-adamantyloxycarbonyl (1-Adoc) group could potentially improve the solubility of amino acids and peptides protected by 1-Adoc in organic solvents due to its strong hydrophobicity.P Lys(l-Adoc) was successfully employed in the synthesis of peptide histidine isoleucine (PHI) (Scheme 9)P9 and in the synthesis of a peptide fragment of a lysozyme.P l... 

Greenberg, B., Rhoden, K. and Barnes, P.J. (1987). Relaxant eflfects of vasoactive intestinal peptide and peptide histidine isoleucine in human and bovine pulmonary arteries. Blood Vessels 24, 45-50. 

PHI Peptide histidine isoleucine PHM Peptide histidine methionine Pi Inorganic phosphate PI Phosphatidylinositol PI-3,4-P2 Phosphatidylinositol 3, 4-biphosphate... 

Limited and/or weak staining is seen at select sites and in select species for a variety of other peptide antisera (e.g., peptide histidine-isoleucine, calcitonin gene-related peptide, the tachykinin family members substance P and neurokinin A, etc. (22, 55, 91, 99)). These various immunoreactivities, though not necessarily prominent in extent or amount, nevertheless suggest the presence of a wide diversity of potentially bioactive peptides in the nervous system of parasitic flatworms. This neurochemical complexity is illustrated in cestodes where 20 different peptide immunoreactivities outnumber the seven putative classical (small molecule) transmitters reported to date for this group in the trematodes there are approximately 24 different peptide immunoreactivities in a wide range of species. These numbers will no doubt continue to increase. 

Borsook s Peptide A. Borsook et al. (85) by chromatography on starch isolated from the liver of numerous animals a peptide whose behavior is such that it seems to be a pure peptide. They gave the name peptide A to it, and described its principal properties (86). This seems to be the same peptide found by Awapara et al. (217). It contains the following amino acids alanine, arginine, aspartic acid, glutamic acid, glycine, histidine, isoleucine, leucine, lysine, methionine, proline, serine, threonine, tryptophan, and tyrosine. 

It is interesting to note that aspartic acid and/or asparagine and glutamic acid and/or glutamine form part of the peptides of all the wine fractions of different studies, independently of the type of wine or the analytical methodology employed in the analysis. Serine, threonine, alanine and glycine appear in most of the fractions studied while, lysine, tyrosine, valine, leucine, histidine and isoleucine has been found in a minor extent in these fractions. 

For example, the leader peptide for the phenylalanine operon includes 7 phenylalanine residues among 15 residues. The threonine operon encodes enzymes required for the synthesis of both threonine and isoleucine the leader peptide contains 8 threonine and 4 isoleucine residues in a 16-residue sequence. The leader peptide for the histidine operon includes 7 histidine residues in a row. In each case, low levels of the corresponding charged tRNA causes the ribosome to stall, trapping the nascent mRNA in a state that can form a structure that allows RNA polymerase to read through the attenuator site. 

Clinton (1986) lists, in decreasing quantitative order, the amino acids and peptides present in a coffee beverage glutamic acid, glycine, aspartic acid, alanine, leucine, valine, isoleucine, serine, phenylalanine, threonine, tyrosine, histidine and y-aminobutyric acid. 

Similar nanotube types were also prepared form peptide amphiphiles made of a hydrophilic head with one or two charged amino acids and a hydrophobic tail of four or more consecutive hydrophobic ones. Between the studied hydrophobic amino acids, alanine and valine produce more homogeneous and stable nanotubes than glycine, isoleucine, and leucine. On the other hand, lysine or histidine is preferred over arginine, possibly due to steric effects. The tubes are stabilized mainly by the hydrophobic effects similar to the LNTs, albeit the diameter is around an order of magnitude smaller. Unlike conventional surfactants. 

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