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Chymotryptic activity

Koslha, V, and F. H. Carpenter Inhibition of chymotryptic activity in crvstalline trvpsin preparations. Journ, Biol. Chem. 239, 1799—1803 (1964). [Pg.37]

EGCG selectively inhibits the activity of topoisomerase 1 but not topoisomerase 11 in human colon cancer cell lines the doses necessary for this inhibition (10-17 pM) are lower than those required for inhibition of cell growth (IC50 = 10-90 pM). EGCG has been shown to inhibit the chymotryptic activity of the 20s proteasome in leukemic, breast cancer, and prostate cancer cell lines, leading to accumulation of p27 P and IkB, and subsequent cell cycle arrest and inhibition of NF-kB activity, respectively. [Pg.169]

Carboxypeptidase B (Worthington COB-DFP, 3.4. 2.2) contained 2. 4 mg enzyme protein per ml. Activity was measured according to Folk et al. (11) using hippuryl-L-arginine (HLA, Sigma) as a substrate. The initial reaction velocities were measured at 254 mu on a Beckman DU spectrophotometer. The enzyme was tested for lack of chymotryptic activity on acetyl-L-tyrosine ethyl ester (obtained through the courtesy of Dr. S. Iwanaga) (12). [Pg.627]

Yasueda H, Mita H, Akiyama K, Shida T, Ando T, Sugiyama S, Yamakawa H. Allergens from Dermatophagoides mites with chymotryptic activity. Clin Exp Allergy 1993 23 384-390. [Pg.514]

Kamath, V., Niketh, S., Chandrashekar, A., and Rajini, P. S. (2007). Chymotryptic hydrolysates of a-kafirin, the storage protein of sorghum (Sorghum bicolor) exhibited angiotensin converting enzyme inhibitory activity. Food Chem. 100, 306-311. [Pg.258]

Watkinson, A., Harding, C., Moore, A., and Coan, P. Water modulation of stratum corneum chymotryptic enzyme activity and desquamation. Arch. Dermatol. Res. 293, 470-476 (2001). [Pg.470]

Sugatani J, Miwa M, Hanahan DJ. Platelet-activating factor stimulation of rabbit platelets is blocked by serine protease inhibitor (chymotryptic protease inhibitor). J Biol Chem 1987 262 5740-5747... [Pg.140]

Domain 4 contains the high-affinity actin binding sites that are involved in inhibition of the actin filament s activity. CD fragment 606C (Marston and Redwood 1992) (Fig. 4), the equivalent chymotryptic fragments ("18K" and "20K") (Szpacenko and Dabrowska,... [Pg.81]

The allergenic character (Fig. 4) of the a-chymotryptic and a-chy-motryptic-tryptic hydrolysate of buffalo s milk proteins and their a-chymotryptic EPM products with different Met enrichments was significantly reduced compared to the unmodified buffalo s milk proteins [105], The most essential decrease in the allergenic activity was found in the a-chymotryptic EPM samples with Met enrichment, probably due to the alteration of the sequential and conformational determinants of the proteins according to the transpeptidation and co-... [Pg.161]

Figure 4 Allergenic activity of the EPM products produced from different proteolytic hydrolysates of buffalo s milk proteins. (I) Buffalo s milk proteins (control) (2) EPM product produced from the chymotryptic hydrolysate without amino acid enrichment (3,4,5,6,7) (a-chymotryptic) EPM products with different Met enrichments (8) a-chymotryptic product produced from the a-chymotryptic and tryptic hydrolysate (without amino acid enrichment) (9,l0,l 1,12,13) a-chymotryptic EPM products with different Met enrichments produced from a peptic and tryptic hydrolysate of buffalo milk proteins. The allergenic activity of the samples was measured in vitro by competitive indirect ELISA. Figure 4 Allergenic activity of the EPM products produced from different proteolytic hydrolysates of buffalo s milk proteins. (I) Buffalo s milk proteins (control) (2) EPM product produced from the chymotryptic hydrolysate without amino acid enrichment (3,4,5,6,7) (a-chymotryptic) EPM products with different Met enrichments (8) a-chymotryptic product produced from the a-chymotryptic and tryptic hydrolysate (without amino acid enrichment) (9,l0,l 1,12,13) a-chymotryptic EPM products with different Met enrichments produced from a peptic and tryptic hydrolysate of buffalo milk proteins. The allergenic activity of the samples was measured in vitro by competitive indirect ELISA.

See other pages where Chymotryptic activity is mentioned: [Pg.70]    [Pg.145]    [Pg.178]    [Pg.33]    [Pg.228]    [Pg.146]    [Pg.163]    [Pg.165]    [Pg.167]    [Pg.66]    [Pg.215]    [Pg.199]    [Pg.201]    [Pg.446]    [Pg.164]    [Pg.70]    [Pg.145]    [Pg.178]    [Pg.33]    [Pg.228]    [Pg.146]    [Pg.163]    [Pg.165]    [Pg.167]    [Pg.66]    [Pg.215]    [Pg.199]    [Pg.201]    [Pg.446]    [Pg.164]    [Pg.135]    [Pg.292]    [Pg.126]    [Pg.42]    [Pg.218]    [Pg.579]    [Pg.21]    [Pg.89]    [Pg.75]    [Pg.130]    [Pg.172]    [Pg.232]    [Pg.220]    [Pg.222]    [Pg.255]    [Pg.283]    [Pg.220]    [Pg.199]    [Pg.393]    [Pg.205]    [Pg.567]    [Pg.5]    [Pg.140]    [Pg.548]   
See also in sourсe #XX -- [ Pg.215 ]




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