NEW SYNTHETIC SUBSTRATES FOR PEPSIN
نویسندگان
چکیده
منابع مشابه
New synthetic substrates for pepsin.
All synthetic substrates for pepsin described heretofore (l-3) have been found to be hydrolyzed maximally near pH 4 at a relatively slow rate. It is now possible to describe synthetic substrates hydrolyzed much more rapidly by pepsin, with a pH optimum at 1.8 to 2.0, the same pH found to be optimal for proteins. The previously described synthetic substrates were N-substituted. peptides and some...
متن کاملThe kinetics of the action of pepsin on synthetic substrates.
The pepsin used in the preliminary experiments of this study was prepared from Parke, Davis pepsin by the method of Philpot (2) and was twice recrystallized. It was stored until used under half saturated magnesium sulfate solution at 2”. Pepsin A was prepared from Cudahy pepsin by the fractionation procedure of Herriott, Desreux, and Northrop (3). Its solubility in 0.05 M acetate, pH 4.6, 0.5 s...
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DNA probes for the studies of damaged strand excision during the nucleotide excision repair (NER) have been designed using the novel non-nucleosidic phosphoramidite reagents that contain N-[6-(9-antracenylcarbamoyl)hexanoyl]-3-amino-1,2-propandiol (nAnt) and N-[6-(5(6)-fluoresceinylcarbamoyl)hexanoyl]-3-amino-1,2-propandiol (nFlu) moieties. New lesion-imitating adducts being inserted into DNA s...
متن کاملHydrolysis and transpeptidation of peptide substrates by acetyl-pepsin.
Treatment of swine pepsin with acetylimidazole to acetylate approximately five of its 16 tyrosyl residues causes a significant enhancement of catalytic efficiency (kcat/Km) toward substrates such as dansyl-glycyl-glycyl-L-phenylalanyl-L-phenylalanine 3-(4-pyridyl)propyl ester and benzyloxy-carbonyl-(glycyl)n-p-nitroLphenylalnyl-Lphenylalanyl-L-tyrosine (where n = 0, 1,2). Stopped-flow kinetic s...
متن کاملThe kinetics of hydrolysis of some synthetic substrates containing neutral hydrophilic groups by pig pepsin and chicken liver cathepsin D.
1. Several peptides containing either of the sequences -Phe(NO2)-Trp- and -Phe(NO2)-Phe- and an uncharged hydrophilic group were synthesized, and the steady-state kinetics of their hydrolysis by pig pepsin (EC 3.4.23.1) and chicken liver cathepsin D (EC 3.4.23.5) were determined. Despite the presence of a hydrophilic group to increase substrate solubility, it was not possible to achieve the con...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1951
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)50936-4