Enzymatic hydrolysis of water-soluble random copolypeptides
β Scribed by Toshio Hayashi; Yasuko Iizuka; Masanao Oya; Makoto Iwatsuki
- Book ID
- 102737505
- Publisher
- John Wiley and Sons
- Year
- 1991
- Tongue
- English
- Weight
- 577 KB
- Volume
- 43
- Category
- Article
- ISSN
- 0021-8995
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β¦ Synopsis
Two component water-soluble random copolypeptides consisting of N-hydroxyethyl L-glutamine and hydrophobic L-amino acids such as L-alanine, L-leucine, L-phenylalanine, or L-valine, were prepared by carrying out aminolysis reactions with 2-amino-1-ethanol (E) on starting copolymers consisting of y-benzyl L-glutamate ( B ) and the corresponding hydrophobic L-amino acid. The effects of copolymer composition and sequential distributions, as well as molecular conformations, on the rate of degradation by bromelain in a PECF at pH 7.4 and 37.0"C to simulate in uiuo polymer degradation. All the samples were found to be extensively degraded by random chain fracture with bromelain. Further, the degradation data for these samples followed the Michaelis-Menten rate law, being of the first order in papain concentration. The nature of side chains and the molecular conformations are important to the rate of degradation by bromelain.
π SIMILAR VOLUMES
Enzymatic hydrolysis rates were determined for different positional and structural esters of lincomycin in dog serum and simulated intestinal fluid USP. In general, the hydrolysis rates were faster in simulated intestinal Auid than in dog serum, indicating a higher esterase activity in simulated int
The synthesis and some of the physical-chemical properties of tricopolymers of L-glutamic acid, blysine, and L-alanine are reported here. The molar ratios of the \* Amino acid analyses of these polypeptides yielded values within approximately 3.5% of the mole ratios of NCA's incorporated into the po