Proteolytic mapping

Yao, Z. P. Demirev, P. A. Fenselau, C. Mass spectrometry-based proteolytic mapping for rapid virus identification. Anal. Chem. 2002, 74, 2529-2534. 

The seven activities of animal FASs are encoded as separate domains of a single 250 kDa polypeptide (Fig. 2) [30, 31]. These include a -ketoacyl synthase, malonyl/acetyl transferase, -ketoreductase, dehydratase, enoyl reductase, and an ACP domain with a phosphopantetheinylated serine. In addition to these activities, the animal FAS also includes a thioesterase domain which cleaves the product fatty acid from the enzyme. Proteolytic mapping of the polypeptide and genetic analysis have defined the location of the various domains in the primary sequence [30,31]. 

Van Vhet K, Blouin V, Agbandje-McKenna M, Snyder RO. Proteolytic mapping of the adeno-associated virus capsid. Mol Ther 2006 14 809-821. 

Luo, K., Hurley, T., and Sefton, B. M. (1990) Transfer of proteins to membranes facilitates both cyanogen bromide cleavage and two-dimensional proteolytic mapping. Oncogene 5, 921-923. 

English, R. D. Warscheid, B. Fenselau, C. Cotter, R. J. Bacillus spore identification using proteolytic mapping and a miniaturized MALDI TOF mass spectrometer. Anal Chem. 2003, 75, 6886-6893. 

The biochemical mechanism of Mos action is not yet established. Mos has been found to phosphorylate cyclin B in vitro, and it is possible that this phosphorylation directly inhibits cyclin B proteolysis (Roy et al., 1990). However, such a direct effect of phosphorylation on cyclin B stability remains to be demonstrated, and it is alternatively possible that Mos inhibits (directly or indirectly) the proteolytic pathway responsible for cyclin B degradation. Mos has recently been found to stimulate mitogen-activated protein kinase (MAP kinase) in Xenopus oocytes,... 

The G-protein that has been termed Gp, and that is linked to phospholipase C activation, may in fact be Gaj 2 or Gc. 3. Ga is designated as the G-protein responsible for activation of phospholipase A2, which results in arachidonic acid release. Some experimental evidence indicates that, at least in HL-60 cells, different agonists can preferentially activate different phospholipases, and some of these are responsible for the activation of secretion. In neutrophils, the two pertussis-toxin-sensitive Ga-proteins (Gaj-2 and G j 3) have been identified by peptide mapping of proteolytic digests of the proteins, by peptide sequencing and by immunoblotting. Complementary-DNA clones for the mRNA of these two molecules have also been isolated from an HL-60 cDNA library. Gai-2 is five to ten times more abundant than Gai.3, the former component comprising 3% of the total plasma membrane proteins. It is possible that these two different Ga-subunits are coupled to different phospholipases (e.g. phospholipases C and D). Pertussis toxin inhibits the secretion of O2 after stimulation of neutrophils by fMet-Leu-Phe, but pertussis-toxin-insensitive G-proteins are also present in neutrophils. These may be members of the Gq family and may be involved in the activation of phospholipase Cp (see 6.3.1). 

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