Powerful adjuvants to augment vaccine efficacy with a less immunogenic vaccine system are in great demand. In this study, a novel squalene-based cationic poly(amino acid) adjuvant (CASq) that elicits both cellular (Th1) and humoral (Th2) immune responses is developed. CASq
Biochemical and biophysical research communications, 546, 35-39 (2021-02-10)
Most of the currently approved therapeutic antibodies are of the immunoglobulin gamma (IgG) κ isotype, leaving a vast opportunity for the use of IgGλ in medical treatments. The incorporation of designer amino acids into antibodies enables efficient and precise manufacturing
The enzymes responsible for the conversion of N(alpha)-[(benzyloxy)carbonyl]-D-lysine (N(alpha)-Z-D-lysine) to N(alpha)-Z-D-aminoadipic acid (N(alpha)-Z-D-AAA) by Rhodococcus sp. AIU Z-35-1 were identified. N(alpha)-Z-D-Lysine was first converted to N(alpha)-Z-D-aminoadipic delta-semialdehyde (N(alpha)-Z-D-AASA) by D-specific amino acid deaminase, whereas N(alpha)-Z-L-lysine was converted to N(alpha)-Z-L-AASA by
The Journal of biological chemistry, 258(3), 1650-1655 (1983-02-10)
Cathepsin B has been shown to catalyze the transfer of the N alpha-benzyloxycarbonyl-L-lysyl residue from the corresponding p-nitrophenyl ester substrate to water and dipeptide nucleophiles. These reactions occurred through the formation of an acyl-enzyme intermediate. The pH dependency of the
Journal of bioscience and bioengineering, 104(3), 218-223 (2007-10-30)
An oxidase catalyzing conversion of N(alpha)-benzyloxycarbonyl-L-lysine (N(alpha)-Z-L-lysine) to N(alpha)-benzyloxycarbonyl-L-aminoadipate-delta-semialdehyde (N(alpha)-Z-L-AASA) was purified from Rhodococcus sp. AIU Z-35-1, and its properties were revealed. This enzyme catalyzed an oxidative deamination of the epsilon-amino group of N(alpha)-acyl-L-lysine and the alpha-amino group of N(epsilon)-acyl-L-lysine.
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