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Amino binding

Iwami, K. and Yasumoto, K. 1986. Amino-binding capacities of food proteins in transglutaminase reaction and digestibility of wheat gliadin with s-attached lysine. J. Sci. Food Agric. 37, 495-503. [Pg.64]

There are a few documented examples of studies of ligand effects on hydrolysis reactions. Angelici et al." investigated the effect of a number of multidentate ligands on the copper(II) ion-catalysed hydrolysis of coordinated amino acid esters. The equilibrium constant for binding of the ester and the rate constant for the hydrolysis of the resulting complex both decrease in the presence of ligands. Similar conclusions have been reached by Hay and Morris, who studied the effect of ethylenediamine... [Pg.76]

Table 3.2. Influence of several -amino acid ligands on the equilibrium constant for binding of 3.8c... Table 3.2. Influence of several -amino acid ligands on the equilibrium constant for binding of 3.8c...
Table 3.5. G, 711 and 7S for the binding of 3.8c to different copper(II)-amino acid complexes in water at 25 C at pH 5-6. Table 3.5. G, 711 and 7S for the binding of 3.8c to different copper(II)-amino acid complexes in water at 25 C at pH 5-6.
Amino-5 -deoxy-2, 3 -0-isopropylideneadenosine was acylated at N-5 with an activated derivative of the 6-carboxy-2-naphthyl ester of Kemp s acid imide. The resulting molecule possesses self-complementary binding sites, the key feature of replicating molecules that act as templates for their own reproduction. The dimer of this molecule is, however, not very stable K = 630 L mol ). When the two initially mentioned educts are added, a small proportion of the ternary complex is also formed and undergoes a fast, template-catalysed... [Pg.347]

Two domains, t1 and t2, exist which affect the GR post-DNA binding transcription activity (37). The major (t1) transactivation domain is 185 amino acid residues ia length with a 58-tesidue a-heUcal functional cote (38). The t1 domain is located at the N terminus of the proteia the minor (t2) trans activation domain residues on the carboxy-terminal side of the DNA binding domain. [Pg.98]

Amino and Phenolic Resins. The largest use of formaldehyde is in the manufacture of urea—formaldehyde, phenol—formaldehyde, and melamine—formaldehyde resins, accounting for over one-half (51%) of the total demand (115). These resins find use as adhesives for binding wood products that comprise particle board, fiber board, and plywood. Plywood is the largest market for phenol—formaldehyde resins particle board is the largest for urea—formaldehyde resins. Under certain conditions, urea—formaldehyde resins may release formaldehyde that has been alleged to create health or environmental problems (see Amino RESINS AND PLASTICS). [Pg.497]

P-Endorphin. A peptide corresponding to the 31 C-terminal amino acids of P-LPH was first discovered in camel pituitary tissue (10). This substance is P-endorphin, which exerts a potent analgesic effect by binding to cell surface receptors in the central nervous system. The sequence of P-endorphin is well conserved across species for the first 25 N-terminal amino acids. Opiates derived from plant sources, eg, heroin, morphine, opium, etc, exert their actions by interacting with the P-endorphin receptor. On a molar basis, this peptide has approximately five times the potency of morphine. Both P-endorphin and ACTH ate cosecreted from the pituitary gland. Whereas the physiologic importance of P-endorphin release into the systemic circulation is not certain, this molecule clearly has been shown to be an important neurotransmitter within the central nervous system. Endorphin has been invaluable as a research tool, but has not been clinically useful due to the avadabihty of plant-derived opiates. [Pg.175]


See other pages where Amino binding is mentioned: [Pg.246]    [Pg.573]    [Pg.698]    [Pg.37]    [Pg.47]    [Pg.377]    [Pg.246]    [Pg.573]    [Pg.698]    [Pg.37]    [Pg.47]    [Pg.377]    [Pg.2814]    [Pg.2826]    [Pg.2826]    [Pg.2827]    [Pg.2836]    [Pg.2843]    [Pg.48]    [Pg.588]    [Pg.602]    [Pg.617]    [Pg.657]    [Pg.75]    [Pg.87]    [Pg.98]    [Pg.100]    [Pg.101]    [Pg.102]    [Pg.162]    [Pg.221]    [Pg.245]    [Pg.77]    [Pg.315]    [Pg.333]    [Pg.48]    [Pg.98]    [Pg.184]    [Pg.188]    [Pg.191]    [Pg.205]    [Pg.211]    [Pg.536]    [Pg.106]    [Pg.254]    [Pg.43]    [Pg.45]    [Pg.45]    [Pg.176]   
See also in sourсe #XX -- [ Pg.17 ]




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