Proteolysis limited

Enzymatic Mild coupling under aqueous conditions without the need for sidechain protection Competing proteolysis limits usefulness... 

Neurokinin effects are terrninated by proteolysis. In vitro acetylcholinesterase (ACE) and enkephalinase can hydrolyze substance P. However, there appears to be no clear evidence that either acetylcholinesterase or ACE limit the actions of released substance P. Enkephalinase inhibitors, eg, thiorphan, can augment substance P release or action in some systems but the distribution of enkephalinase in the brain does not precisely mirror that of substance P. There appears to be a substance P-selective enzyme in brain and spinal cord. 

Roberts, L. M., Ray, M. J., Shih, T. W., et al., 1997. Strnctnral analy.sis of apolipoprotein A-I Limited proteolysis of methionine-rednced and -oxidized lipid-free and lipid-bonnd human Apo A-I. Biochemistry 36 7615. 

Regulation of Anti-HIV Properties of Chemokines by Limited Proteolysis... 

Vaughan, R. A. and Kuhar, M. J. (1996) Dopamine transporter ligand binding domains. Structural and functional properties revealed by limited proteolysis. J. Biol. Chem. 271, 21672-21680. 

McKinley, M. P., Meyer, R. K, Kenaga, L., Rahbar, F., Cotter, R., Serban, A., and Prusiner, S. B. (1991). Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis./ Virol. 65, 1340-1351. 

This enzyme (RNase A) is a single chain protein of 124 amino acid residues, cross-linked by four intrachain disulfide bonds. Limited proteolysis of the enzyme cuts a single peptide bond between residues 20 and 21 (Richards and Vithayathil, 1959). The derived protein, RNase S, retains enzymic activity although the N-terminal peptide of 20 amino acids (S-peptide) is no longer covalently attached to the balance of the molecule (S-protein). Removal of S-peptide from... 

In a further study, Taniuchi et al. (1977) have shown that in the association of overlapping fragments of staphylococcal nuclease, two different species of active enzyme are formed. On the basis of the products of limited proteolysis, structures for the two species were deduced. In one case a structure is proposed in which fragment 1-126 assumes native-like structure over the sequence 1-48, and all of fragment 50-149 assumes native-like structure. In the other case the structure is one in which fragment 1-126 assumes native-like structure over the sequence 1-110, while that part of fragment 50-149 in the sequence interval 111-149 assumes native-like structure. The interest of these results is enhanced by the finding that the two active species initially form in relative concentrations substantially different from their equilibrium concentrations. Thus, both a mobile equilibrium and substantial kinetic control of the early products are evident. Taniuchi et al. did not reach a clear-cut mechanistic conclusion from their studies. 

In a more limited study, Johnson (1974) studied the —S—S— pairing in the oxidative regeneration of reduced lysozyme peptide 57-83. By limited proteolysis and fractionation of the resultant pep-... 

Limited proteolysis. Flexible regions of proteins can sometimes be removed by digestion of the protein with different proteases. This technique is based on the techniques that were used to determine the core folded regions of proteins, most notably antibodies (Porter, 1973). Limited proteolysis can be used to remove flexible loops of proteins, or separate multidomain proteins into separate domains and has been used successfully in a number of instances (Noel et al., 1993 Sondek et al., 1996 Mazza et al., 2002). 

---