Peptide, sequencing C-terminal

Triazolo[3,4-a ]phthalazine C-Terminal peptide sequencing 78DIS(B)(39)233... 

Laughlin MJ, Chantler SE, Okita TW. N- and C-terminal peptide sequences are essential for enzyme assembly, allosteric, and/or catalytic properties of ADP-glucose pyrophosphorylase. Plant J. 1998 14 159-168. 

Lin, T. Payne, A.H. Glish, G.L. Dissociation pathways of aUcali-cationized peptides Opportunities for C-terminal peptide sequencing. J. Am. Soc. Mass Spectrom. 2001,12, 497-504. 

Lin T, Glish GL. C-terminal peptide sequencing via multistage mass spectrometry. Anal Chem. 1998 70 5162 5. 

Although the protein products of these mRNAs differ in their C-terminal peptide sequence and capacity to oligomerize, all of the molecular forms of AChE carry an identical active site and display similar catalytic properties. Importantly, the distinct C-termini dictate dissimilar subcellular localizations, biological roles, and noncatalytic properties. 

The gene encoding PBAN was first characterized from H. zea and B. mori [134,137,138,195]. The cDNA was found to encode the 33 amino acid PBAN plus four additional peptides with a common C-terminal FXPRL sequence motif, including that of the diapause hormone of B. mori (Fig. 6). Three additional peptides with the common C-termini and sequence homology to those of H. zea and B. mori have been deduced from cDNA isolated from pheromone glands of several other moths [194,196-200]. Studies conducted to find the post-translational processed peptides indicated that PBAN was found to a greater extent in the mandibular and maxillary clusters than in the labial cluster of neurons... 

Fig. 6 Sequence alignment of the deduced amino acid sequence from the identified cDNA encoding PBAN and related peptides from Helicoverpa zea and Bombyx mori. The putatively expressed peptides are shown in boxes. The conserved amino acids are underlined in the B. mori sequence. Putative proteolytic posttranslational processing sites are shown in bold with glycine contributing the C-terminal amide. Sequences of PBAN-like peptides are also shown in Table 1. GenBank accession numbers H. zea - PI 1159 and B. mori - BAA05971...

Lins et al. 127 have studied five peptide sequences derived from the ApoB-100 protein, which is the protein moiety in low-density lipoproteins (LDC) that transport cholesterol. ApoB-100 is insoluble and binds to the surface of the LDC particle, and these selected sequences for this study have been implicated as being important in the lipid binding. ATR-FTIR studies showed the one core and three C-terminal originating sequences were mostly sheet-like in the presence of unilamellar vesicles but the N-terminal one was different, probably representing a complex mixture of conformers with some helical component. Furthermore, these workers were able to carry out ATR-LD measurements and determine the orientation of the peptide as being oblique to the membrane. These studies are in contrast to ultraviolet ECD results which were adversely affected by scattering artifacts. 

Adrenomedullin (AM) was first discovered in human adrenal medullary pheochromocytoma tissue. It is a 52-amino acid peptide with a six-amino-acid ring and a C-terminal amidation sequence. Like CGRP, AM is a member of the calcitonin family of peptides. 

Finally, the C-terminal peptide of the 5-HT4b receptors was unable to retain any specific protein, consistent with the lack of any identified interaction motif in its sequence. 

Recently Moody et al.,22) discovered that the C-terminal partial sequence of bombesin and bombesin-like peptides (BLPs) can function as autocrine growth factors in human small-cell lung cancer (SCLC) cell lines. 

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